ARO10 (YDR380W) encodes a cytosolic thiamine-diphosphate- and Mg2+-dependent 2-oxo-acid decarboxylase of the pyruvate decarboxylase family that catalyses the decarboxylation step of the Ehrlich pathway, converting transaminated amino acids into the corresponding aldehydes, which are then reduced to fusel alcohols or oxidised to fusel acids. Its preferred substrates are the aromatic 2-oxo acids phenylpyruvate, indole-3-pyruvate and 4-hydroxyphenylpyruvate, making it the physiologically relevant phenylpyruvate decarboxylase; it also decarboxylates branched-chain (4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate) and sulfur-containing (4-methylthio-2-oxobutanoate) 2-oxo acids with high affinity, contributing to isoamyl alcohol, active amyl alcohol and methionol formation. Unlike its paralogs PDC1/5/6 it cannot decarboxylate pyruvate. ARO10 transcription is induced by aromatic amino acids via Aro80 and when phenylalanine, leucine or methionine is the nitrogen source.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000287 magnesium ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro IPR012000 (TPP enzyme central domain) mapping to magnesium ion binding; TPP-dependent 2-oxo-acid decarboxylases bind Mg2+ that anchors the diphosphate of ThDP. Cofactor binding is inferred by homology for ARO10. Reason: Correct cofactor binding for this enzyme family. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Note=Binds 1 Mg(2+) per subunit. |
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro IPR011766 mapping to the root "catalytic activity"; correct but uninformative. Reason: Too general; the specific activity is aromatic 2-oxo-acid (phenylpyruvate) decarboxylation. Proposed replacements: phenylpyruvate decarboxylase activity Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2; PMID:12902239 ARO10 was sufficient to encode phenylpyruvate decarboxylase activity in the absence of the four other candidate genes |
| GO:0004737 pyruvate decarboxylase activity | IBA GO_REF:0000033 | REMOVE | Summary: PAINT IBA transferring pyruvate decarboxylase activity from the PDC clade (PDC1/5/6). ARO10 has diverged within this family into an aromatic/branched-chain 2-oxo-acid decarboxylase: purified Aro10 cannot decarboxylate pyruvate, and when each decarboxylase was overexpressed in a quintuple-null strain only Pdc1, Pdc5 and Pdc6 decarboxylated pyruvate and other linear-chain 2-oxo acids. Reason: Target-specific loss of the ancestral pyruvate activity is experimentally demonstrated. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN008451158 · PTN008451158 SUPPORTS SOURCE BUT NOT TARGET Pyruvate decarboxylase activity is well supported for PDC1/PDC5/PDC6, but ARO10 has diverged to aromatic/branched-chain 2-oxo acids and does not decarboxylate pyruvate. Supporting Evidence: PMID:22904058 Aro10, which cannot decarboxylate pyruvate, exhibited clear Michaelis-Menten-type saturation kinetics for all other substrates tested PMID:22904058 only Pdc1, Pdc5, and Pdc6 catalyzed the decarboxylation of the linear-chain 2-oxo acids pyruvate, 2-oxo-butanoate, and 2-oxo-pentanoate in cell extracts file:yeast/ARO10/ARO10-uniprot.txt low efficiency substrate and transaminated valine and pyruvate are no |
| GO:0004737 pyruvate decarboxylase activity | IEA GO_REF:0000116 | REMOVE | Summary: Rhea-to-GO mapping (GO_REF:0000116) from RHEA:54360, which is actually the decarboxylation of 4-methyl-2-oxopentanoate to 3-methylbutanal (EC 4.1.1.72), not of pyruvate. ARO10 does not decarboxylate pyruvate. Reason: Incorrect mapping; activity experimentally excluded for ARO10. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=4-methyl-2-oxopentanoate + H(+) = 3-methylbutanal + CO2; PMID:22904058 Aro10, which cannot decarboxylate pyruvate, exhibited clear Michaelis-Menten-type saturation kinetics for all other substrates tested |
| GO:0005634 nucleus | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: PAINT IBA for nucleus on a node including PDC1 and PDC5. There is no evidence for nuclear localisation or nuclear function of ARO10; HTP localisation places it in the cytoplasm/cytosol. Reason: Nuclear location not supported for ARO10. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: PANTHER:PTN001056938 · PTN001056938 SUPPORTS SOURCE BUT NOT TARGET Nuclear signal reported for PDC isozymes is not reproduced for ARO10, which HTP screens place in cytoplasm/cytosol. Supporting Evidence: PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories PMID:26928762 we developed a SWAp-Tag (SWAT) method that enables one parental library to be modified easily and efficiently |
| GO:0005737 cytoplasm | HDA PMID:14562095 Global analysis of protein localization in budding yeast. | ACCEPT | Summary: Genome-wide GFP localisation scored ARO10 as cytoplasmic; consistent with its role in cytosolic Ehrlich-pathway catabolism. Reason: Consistent localisation. Supporting Evidence: PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt SubCell "Cytoplasm" mapping; correct, though cytosol is more specific. Reason: Correct location. Supporting Evidence: PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | ACCEPT | Summary: SWAT-GFP high-throughput localisation scored ARO10 in the cytosol. Reason: Consistent localisation. Supporting Evidence: PMID:26928762 we developed a SWAp-Tag (SWAT) method that enables one parental library to be modified easily and efficiently |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA placing TPP-dependent 2-oxo-acid decarboxylases in the cytosol; consistent with HTP data for ARO10. Reason: Correct location. Supporting Evidence: PMID:26928762 we developed a SWAp-Tag (SWAT) method that enables one parental library to be modified easily and efficiently |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA placing the Ehrlich-pathway decarboxylation steps (Trp, Ile, Leu, Phe degradation) in the cytosol; consistent with HTP localisation of ARO10. Reason: Correct compartment. Supporting Evidence: PMID:26928762 we developed a SWAp-Tag (SWAT) method that enables one parental library to be modified easily and efficiently PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA placing the Ehrlich-pathway decarboxylation steps (Trp, Ile, Leu, Phe degradation) in the cytosol; consistent with HTP localisation of ARO10. Reason: Correct compartment. Supporting Evidence: PMID:26928762 we developed a SWAp-Tag (SWAT) method that enables one parental library to be modified easily and efficiently PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA placing the Ehrlich-pathway decarboxylation steps (Trp, Ile, Leu, Phe degradation) in the cytosol; consistent with HTP localisation of ARO10. Reason: Correct compartment. Supporting Evidence: PMID:26928762 we developed a SWAp-Tag (SWAT) method that enables one parental library to be modified easily and efficiently PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA placing the Ehrlich-pathway decarboxylation steps (Trp, Ile, Leu, Phe degradation) in the cytosol; consistent with HTP localisation of ARO10. Reason: Correct compartment. Supporting Evidence: PMID:26928762 we developed a SWAp-Tag (SWAT) method that enables one parental library to be modified easily and efficiently PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0006550 L-isoleucine catabolic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (isoleucine degradation, PWY3O-4109) placing ARO10 at the (S)-3-methyl-2-oxopentanoate decarboxylation step. Dickinson et al. (2000) showed any one of PDC1/5/6, THI3 or YDR380w (ARO10) suffices for isoleucine catabolism to active amyl alcohol, and Aro10 has high affinity for branched-chain 2-oxo acids. Reason: The enzyme performs the decarboxylation step of isoleucine catabolism (redundantly). Supporting Evidence: PMID:10753893 Apparently, any one of this family of decarboxylases is sufficient to allow the catabolism of isoleucine to active amyl alcohol. PMID:10753893 This is the first demonstration of a role for the gene product of YDR380w PMID:22904058 The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols. file:yeast/ARO10/ARO10-uniprot.txt Reaction=(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2; |
| GO:0006552 L-leucine catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Dickinson et al. (2003) analysed leucine catabolism in combinatorial decarboxylase mutants and found Ydr380wp (ARO10) acts as a decarboxylase of alpha-ketoisocaproate (minor relative to the other isozymes in their background); later chemostat and kinetic work identifies Aro10 as a key contributor to branched-chain fusel alcohols. Reason: Genetic evidence that ARO10 performs the decarboxylation step of leucine catabolism. Supporting Evidence: PMID:12499363 We also report that in leucine catabolism Ydr380wp is the minor decarboxylase. PMID:22904058 The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols. PMID:15933030 Constitutive expression of ARO10 in this genetic background (strain IMZ002) restored decarboxylase activity with the 2-oxo acids derived from leucine, phenylalanine, and methionine. |
| GO:0006552 L-leucine catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Dickinson et al. (2003) analysed leucine catabolism in combinatorial decarboxylase mutants and found Ydr380wp (ARO10) acts as a decarboxylase of alpha-ketoisocaproate (minor relative to the other isozymes in their background); later chemostat and kinetic work identifies Aro10 as a key contributor to branched-chain fusel alcohols. Reason: Genetic evidence that ARO10 performs the decarboxylation step of leucine catabolism. Supporting Evidence: PMID:12499363 We also report that in leucine catabolism Ydr380wp is the minor decarboxylase. PMID:22904058 The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols. PMID:15933030 Constitutive expression of ARO10 in this genetic background (strain IMZ002) restored decarboxylase activity with the 2-oxo acids derived from leucine, phenylalanine, and methionine. |
| GO:0006552 L-leucine catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Dickinson et al. (2003) analysed leucine catabolism in combinatorial decarboxylase mutants and found Ydr380wp (ARO10) acts as a decarboxylase of alpha-ketoisocaproate (minor relative to the other isozymes in their background); later chemostat and kinetic work identifies Aro10 as a key contributor to branched-chain fusel alcohols. Reason: Genetic evidence that ARO10 performs the decarboxylation step of leucine catabolism. Supporting Evidence: PMID:12499363 We also report that in leucine catabolism Ydr380wp is the minor decarboxylase. PMID:22904058 The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols. PMID:15933030 Constitutive expression of ARO10 in this genetic background (strain IMZ002) restored decarboxylase activity with the 2-oxo acids derived from leucine, phenylalanine, and methionine. |
| GO:0006552 L-leucine catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Dickinson et al. (2003) analysed leucine catabolism in combinatorial decarboxylase mutants and found Ydr380wp (ARO10) acts as a decarboxylase of alpha-ketoisocaproate (minor relative to the other isozymes in their background); later chemostat and kinetic work identifies Aro10 as a key contributor to branched-chain fusel alcohols. Reason: Genetic evidence that ARO10 performs the decarboxylation step of leucine catabolism. Supporting Evidence: PMID:12499363 We also report that in leucine catabolism Ydr380wp is the minor decarboxylase. PMID:22904058 The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols. PMID:15933030 Constitutive expression of ARO10 in this genetic background (strain IMZ002) restored decarboxylase activity with the 2-oxo acids derived from leucine, phenylalanine, and methionine. |
| GO:0006552 L-leucine catabolic process | IMP PMID:10753893 An investigation of the metabolism of isoleucine to active A... | ACCEPT | Summary: Curator IMP from Dickinson et al. (2000), which used decarboxylase mutants to study branched-chain 2-oxo acid catabolism; the abstract reports YDR380w roles for isoleucine and discusses leucine decarboxylation. Consistent with later evidence that ARO10 decarboxylates the leucine-derived 2-oxo acid. Reason: Experimental annotation consistent with independent evidence; abstract-only cache so curator deferred to. Supporting Evidence: PMID:10753893 This is the first demonstration of a role for the gene product of YDR380w PMID:15933030 Constitutive expression of ARO10 in this genetic background (strain IMZ002) restored decarboxylase activity with the 2-oxo acids derived from leucine, phenylalanine, and methionine. |
| GO:0006552 L-leucine catabolic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (leucine degradation, PWY3O-4112) placing ARO10 at the 4-methyl-2-oxopentanoate decarboxylation step; supported by genetic and enzymatic evidence. Reason: Correct pathway step. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=4-methyl-2-oxopentanoate + H(+) = 3-methylbutanal + CO2; PMID:15933030 Constitutive expression of ARO10 in this genetic background (strain IMZ002) restored decarboxylase activity with the 2-oxo acids derived from leucine, phenylalanine, and methionine. |
| GO:0006559 L-phenylalanine catabolic process | IDA PMID:12902239 Identification and characterization of phenylpyruvate decarb... | ACCEPT | Summary: Vuralhan et al. (2003) showed ARO10 is sufficient for phenylpyruvate decarboxylase activity and phenylalanine catabolite (phenylethanol) production in the absence of the other candidate decarboxylases, and is the physiologically relevant phenylpyruvate decarboxylase. Reason: Core process; ARO10 catalyses the first committed step of phenylalanine catabolism via the Ehrlich pathway. Supporting Evidence: PMID:12902239 ARO10 was sufficient to encode phenylpyruvate decarboxylase activity in the absence of the four other candidate genes PMID:12902239 showing that Aro10p is the physiologically relevant phenylpyruvate decarboxylase in wild-type cells PMID:12902239 Analyses of phenylalanine catabolite production and phenylpyruvate decarboxylase enzyme assays |
| GO:0006559 L-phenylalanine catabolic process | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA (ARBA00085541) assignment of L-phenylalanine catabolic process; matches the experimentally established role. Reason: Correct. Supporting Evidence: PMID:12902239 showing that Aro10p is the physiologically relevant phenylpyruvate decarboxylase in wild-type cells |
| GO:0006559 L-phenylalanine catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Combinatorial decarboxylase mutants showed phenylpyruvate decarboxylation in phenylalanine catabolism can be effected by any of Pdc1p, Pdc5p, Pdc6p or Ydr380wp (ARO10). Reason: Genetic evidence for the core process. Supporting Evidence: PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp |
| GO:0006559 L-phenylalanine catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Combinatorial decarboxylase mutants showed phenylpyruvate decarboxylation in phenylalanine catabolism can be effected by any of Pdc1p, Pdc5p, Pdc6p or Ydr380wp (ARO10). Reason: Genetic evidence for the core process. Supporting Evidence: PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp |
| GO:0006559 L-phenylalanine catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Combinatorial decarboxylase mutants showed phenylpyruvate decarboxylation in phenylalanine catabolism can be effected by any of Pdc1p, Pdc5p, Pdc6p or Ydr380wp (ARO10). Reason: Genetic evidence for the core process. Supporting Evidence: PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp |
| GO:0006559 L-phenylalanine catabolic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (phenylalanine degradation, PWY3O-4115) placing ARO10 at the phenylpyruvate decarboxylation step; correct. Reason: Correct pathway step. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2; PMID:12902239 showing that Aro10p is the physiologically relevant phenylpyruvate decarboxylase in wild-type cells |
| GO:0006569 L-tryptophan catabolic process | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA (ARBA00026552) assignment of L-tryptophan catabolic process; consistent with genetic and enzymatic evidence. Reason: Correct. Supporting Evidence: PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. |
| GO:0006569 L-tryptophan catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Combinatorial decarboxylase mutants showed indolepyruvate decarboxylation in tryptophan catabolism to tryptophol can be effected by any of Pdc1p, Pdc5p, Pdc6p or Ydr380wp (ARO10). Reason: Genetic evidence that ARO10 performs the decarboxylation step of tryptophan catabolism. Supporting Evidence: PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. |
| GO:0006569 L-tryptophan catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Combinatorial decarboxylase mutants showed indolepyruvate decarboxylation in tryptophan catabolism to tryptophol can be effected by any of Pdc1p, Pdc5p, Pdc6p or Ydr380wp (ARO10). Reason: Genetic evidence that ARO10 performs the decarboxylation step of tryptophan catabolism. Supporting Evidence: PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. |
| GO:0006569 L-tryptophan catabolic process | IGI PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Combinatorial decarboxylase mutants showed indolepyruvate decarboxylation in tryptophan catabolism to tryptophol can be effected by any of Pdc1p, Pdc5p, Pdc6p or Ydr380wp (ARO10). Reason: Genetic evidence that ARO10 performs the decarboxylation step of tryptophan catabolism. Supporting Evidence: PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. |
| GO:0006569 L-tryptophan catabolic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (tryptophan degradation, PWY3O-214) placing ARO10 at the indole-3-pyruvate decarboxylation step; correct. Reason: Correct pathway step. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=indole-3-pyruvate + H(+) = indole-3-acetaldehyde + CO2; PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. |
| GO:0009087 L-methionine catabolic process | IMP PMID:16423070 Methionine catabolism in Saccharomyces cerevisiae. | ACCEPT | Summary: Perpete et al. showed the decarboxylation of 4-methylthio-2-oxobutanoate to methional in methionine catabolism to methionol is effected specifically by Ydr380wp (ARO10). Kneen et al. questioned a major role from in vitro kinetics, but chemostat and kinetic studies place Aro10 as a key contributor to sulfur-containing fusel alcohols. Reason: Mutant evidence that ARO10 performs the decarboxylation step of methionine catabolism. Supporting Evidence: PMID:16423070 The decarboxylation is effected specifically by Ydr380wp. PMID:22904058 The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols. |
| GO:0016831 carboxy-lyase activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro IPR012110 (pyruvate decarboxylase/indolepyruvate decarboxylase family) mapping to generic carboxy-lyase activity; correct but uninformative. Reason: Too general. Proposed replacements: phenylpyruvate decarboxylase activity Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2; |
| GO:0016831 carboxy-lyase activity | IMP PMID:10753893 An investigation of the metabolism of isoleucine to active A... | MODIFY | Summary: Curator IMP (Dickinson et al. 2000) for generic carboxy-lyase activity based on mutant analysis of 2-oxo acid decarboxylation in isoleucine catabolism; the specific activity is branched-chain 2-oxo-acid decarboxylation, already annotated by EXP from the same paper. Reason: Too general; the specific activity is supported by the same study. Proposed replacements: branched-chain-2-oxoacid decarboxylase activity Supporting Evidence: PMID:10753893 Apparently, any one of this family of decarboxylases is sufficient to allow the catabolism of isoleucine to active amyl alcohol. file:yeast/ARO10/ARO10-uniprot.txt Reaction=(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2; |
| GO:0030976 thiamine pyrophosphate binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro TPP-enzyme domains (IPR011766/IPR012000/IPR012001) mapping to thiamine pyrophosphate binding; ARO10 is a ThDP-dependent decarboxylase. Reason: Correct cofactor binding. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Note=Binds 1 thiamine pyrophosphate per subunit. PMID:21501384 Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae. |
| GO:0047433 branched-chain-2-oxoacid decarboxylase activity | EXP PMID:10753893 An investigation of the metabolism of isoleucine to active A... | ACCEPT | Summary: Dickinson et al. (2000) showed ARO10 (YDR380w) can decarboxylate alpha-keto-beta-methylvalerate in isoleucine catabolism; later kinetics confirm Aro10 decarboxylates branched-chain 2-oxo acids with high affinity. Reason: Experimentally supported activity; secondary to the aromatic substrates in vitro but physiologically relevant for fusel-alcohol formation. Supporting Evidence: PMID:10753893 Apparently, any one of this family of decarboxylases is sufficient to allow the catabolism of isoleucine to active amyl alcohol. PMID:22904058 The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols. |
| GO:0047433 branched-chain-2-oxoacid decarboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (ARBA, RHEA:21108, EC 4.1.1.72) for branched-chain 2-oxoacid decarboxylase activity; consistent with experimental data. Reason: Correct. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2; |
| GO:0047433 branched-chain-2-oxoacid decarboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (isoleucine degradation) for EC 4.1.1.72; correct. Reason: Correct. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2; PMID:22904058 The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols. |
| GO:0047434 indolepyruvate decarboxylase activity | EXP PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Indole-3-pyruvate decarboxylation by ARO10: genetic evidence (Dickinson 2003) and in vitro kinetics of recombinant enzyme (Kneen 2011, Km 0.03 mM) establish efficient indolepyruvate decarboxylase activity. Reason: Core activity for tryptophan catabolism. Supporting Evidence: PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp |
| GO:0047434 indolepyruvate decarboxylase activity | EXP PMID:21501384 Characterization of a thiamin diphosphate-dependent phenylpy... | ACCEPT | Summary: Indole-3-pyruvate decarboxylation by ARO10: genetic evidence (Dickinson 2003) and in vitro kinetics of recombinant enzyme (Kneen 2011, Km 0.03 mM) establish efficient indolepyruvate decarboxylase activity. Reason: Core activity for tryptophan catabolism. Supporting Evidence: PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp |
| GO:0047434 indolepyruvate decarboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (ARBA, RHEA:18017, EC 4.1.1.74); correct. Reason: Correct. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=indole-3-pyruvate + H(+) = indole-3-acetaldehyde + CO2; |
| GO:0047434 indolepyruvate decarboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (tryptophan degradation) for indolepyruvate decarboxylase; correct. Reason: Correct. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=indole-3-pyruvate + H(+) = indole-3-acetaldehyde + CO2; |
| GO:0050177 phenylpyruvate decarboxylase activity | EXP PMID:12499363 The catabolism of amino acids to long chain and complex alco... | ACCEPT | Summary: Phenylpyruvate decarboxylation by ARO10 in combinatorial mutant strains (Dickinson 2003). Reason: Core activity. Supporting Evidence: PMID:12499363 This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp |
| GO:0050177 phenylpyruvate decarboxylase activity | IDA PMID:12902239 Identification and characterization of phenylpyruvate decarb... | ACCEPT | Summary: Enzyme assays showed ARO10 alone supports phenylpyruvate decarboxylase activity and has the physiologically relevant kinetic properties. Reason: Core activity; direct assay. Supporting Evidence: PMID:12902239 ARO10 was sufficient to encode phenylpyruvate decarboxylase activity in the absence of the four other candidate genes PMID:12902239 showing that Aro10p is the physiologically relevant phenylpyruvate decarboxylase in wild-type cells |
| GO:0050177 phenylpyruvate decarboxylase activity | IDA PMID:21501384 Characterization of a thiamin diphosphate-dependent phenylpy... | ACCEPT | Summary: Recombinant Aro10 purified from E. coli is an efficient ThDP-dependent aromatic 2-keto acid decarboxylase, with phenylpyruvate as a preferred substrate. Reason: Core activity; purified enzyme. Supporting Evidence: PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. PMID:22904058 Only Aro10 and Pdc5 catalyzed the decarboxylation of the aromatic substrate phenylpyruvate, with Aro10 showing superior kinetic properties. |
| GO:0050177 phenylpyruvate decarboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (ARBA, RHEA:14185, EC 4.1.1.43); correct. Reason: Correct. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2; |
| GO:0050177 phenylpyruvate decarboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (phenylalanine and leucine degradation pathways). Phenylpyruvate decarboxylase activity is correct for ARO10; the PWY3O-4112 (leucine) row carries this aromatic-substrate term only because the pathway reaction was assigned EC 4.1.1.43, which is a pathway-to-GO mapping quirk but does not make the activity wrong. Reason: Correct activity for the gene product. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2; PMID:22904058 Only Aro10 and Pdc5 catalyzed the decarboxylation of the aromatic substrate phenylpyruvate, with Aro10 showing superior kinetic properties. |
| GO:0050177 phenylpyruvate decarboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (phenylalanine and leucine degradation pathways). Phenylpyruvate decarboxylase activity is correct for ARO10; the PWY3O-4112 (leucine) row carries this aromatic-substrate term only because the pathway reaction was assigned EC 4.1.1.43, which is a pathway-to-GO mapping quirk but does not make the activity wrong. Reason: Correct activity for the gene product. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2; PMID:22904058 Only Aro10 and Pdc5 catalyzed the decarboxylation of the aromatic substrate phenylpyruvate, with Aro10 showing superior kinetic properties. |
| GO:0050546 4-hydroxyphenylpyruvate decarboxylase activity | EXP PMID:21501384 Characterization of a thiamin diphosphate-dependent phenylpy... | ACCEPT | Summary: Kneen et al. measured decarboxylation of 4-hydroxyphenylpyruvate by recombinant Aro10 (Km 0.09 mM), supporting a probable role in tyrosine catabolism to tyrosol. Reason: Experimentally supported activity. Supporting Evidence: PMID:21501384 The enzyme is shown to be an efficient aromatic 2-keto acid decarboxylase, consistent with it playing a major in vivo role in phenylalanine, tryptophan and possibly also tyrosine catabolism. file:yeast/ARO10/ARO10-uniprot.txt Reaction=3-(4-hydroxyphenyl)pyruvate + H(+) = (4- |
| GO:0050546 4-hydroxyphenylpyruvate decarboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (RHEA:18697, EC 4.1.1.80); consistent with experimental data. Reason: Correct. Supporting Evidence: file:yeast/ARO10/ARO10-uniprot.txt Reaction=3-(4-hydroxyphenyl)pyruvate + H(+) = (4- |
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Download this section (compressed HTML)Q: Why does constitutively expressed ARO10 yield no 2-oxo-acid decarboxylase activity in ammonia-grown wild-type cells: post-translational regulation or a required partner protein?
Q: How should GO capture decarboxylation of 4-methylthio-2-oxobutanoate (methionine Ehrlich branch), which has no specific MF term?
Experiment: Test for post-translational modification or partner proteins of Aro10 by affinity purification from phenylalanine- versus ammonia-grown cells, correlating with decarboxylase activity.
Phenylpyruvate decarboxylase; catalyzes decarboxylation of phenylpyruvate to phenylacetaldehyde, which is the first specific step in the Ehrlich pathway; involved in protein N-terminal Met and Ala catabolism
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