CYP71B15

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004497 monooxygenase activity	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: CYP71B15 is a cytochrome P450 enzyme that uses O2 and electrons from NADPH-P450 reductase. Monooxygenase activity is the generic P450 family label, mapped from InterPro. Reason: The label fits the P450 family, but it does not describe the specific chemistry. The two characterised PAD3 reactions (EC 1.14.19.52) reduce O2 to water without a net oxygen atom ending up in the product: Cys(IAN) thiazoline ring closure with cyanide release, and oxidative decarboxylation of dihydrocamalexic acid. The specific activity is captured by GO:0010298 and the proposed dihydrocamalexate synthase term. Kept as a non-core, family-level annotation. Supporting Evidence: PMID:10590168 The predicted PAD3 protein appears to be a cytochrome P450 monooxygenase, similar to those from maize PMID:16766671 CYP71B15 catalyzes an oxidative decarboxylation of both enantiomers of dihydrocamalexic acid PMID:19567706 Surprisingly, yeast-expressed CYP71B15 also catalyzed thiazoline ring closure, DHCA formation, and cyanide release with Cys(IAN) as substrate.
GO:0004497 monooxygenase activity	ISS PMID:10590168 Arabidopsis PAD3, a gene required for camalexin biosynthesis...	KEEP AS NON CORE	Summary: ISS from the original cloning paper, which predicted that PAD3 encodes a cytochrome P450 monooxygenase by similarity to maize benzoxazinoid P450s. Reason: The prediction that PAD3 is a P450 was correct, and biochemistry later confirmed it. As with the IEA row, monooxygenase activity is a generic family label. The experimentally defined activities are more specific: oxidative decarboxylation of DHCA (GO:0010298), and conversion of Cys(IAN) to DHCA, which has no GO term yet. Supporting Evidence: PMID:10590168 The predicted PAD3 protein appears to be a cytochrome P450 monooxygenase, similar to those from maize PMID:16766671 Recombinant CYP71B15 heterologously expressed in yeast catalyzed the conversion of dihydrocamalexic acid to camalexin with preference of the (S)-enantiomer.
GO:0005506 iron ion binding	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: InterPro-based annotation of iron ion binding for a heme-thiolate P450. Reason: In P450s the iron is the heme iron, coordinated within the protoporphyrin and by the conserved cysteine thiolate. The protein binds the heme cofactor, not free iron ions, and that is already captured by heme binding (GO:0020037). Iron ion binding is a redundant mapping artefact. Supporting Evidence: PMID:10590168 The predicted PAD3 protein appears to be a cytochrome P450 monooxygenase, similar to those from maize
GO:0005515 protein binding	IPI PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	REMOVE	Summary: IPI with CYP71A12 (O49340) from the camalexin metabolon co-immunoprecipitation and FRET-FLIM study. Reason: The interaction is real and supports physical organisation of the camalexin pathway P450s into an ER-associated complex; removing the row does not mean the interaction is false. However, "protein binding" says nothing about function, and no more informative MF term fits a metabolon association. The functionally meaningful content, the shared camalexin biosynthetic process and ER localization, is captured elsewhere. Supporting Evidence: PMID:31511315 we used two independent untargeted coimmunoprecipitation (co-IP) approaches with the biosynthetic enzymes CYP71B15 and CYP71A13 as baits and determined that the camalexin biosynthetic P450 enzymes copurified with these enzymes.
GO:0005515 protein binding	IPI PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	REMOVE	Summary: IPI with CYP71A13 (O49342), the upstream camalexin P450, from co-IP with CYP71B15 and CYP71A13 as baits. Reason: The association is well supported (reciprocal untargeted co-IP, targeted co-IP, FRET-FLIM) and points to metabolic channelling; removing the row does not mean the interaction is false. "Protein binding" is still uninformative as a molecular function, and no more specific MF term applies. The biology is captured by camalexin biosynthetic process. Supporting Evidence: PMID:31511315 we used two independent untargeted coimmunoprecipitation (co-IP) approaches with the biosynthetic enzymes CYP71B15 and CYP71A13 as baits and determined that the camalexin biosynthetic P450 enzymes copurified with these enzymes. PMID:31511315 efficiently synthesizes the antifungal phytoalexin camalexin without the apparent release of bioactive intermediates
GO:0005515 protein binding	IPI PMID:33831160 The Formation of a Camalexin Biosynthetic Metabolon.	REMOVE	Summary: IPI with GSTU4 (AT2G29460). The cited PMID:33831160 is a deleted PubMed duplicate of PMID:31511315 (Mucha et al. 2019), the camalexin metabolon study, which shows GSTU4 recruited to the P450 complex by FRET-FLIM and co-IP. Reason: With the duplicate resolved, the source is the metabolon paper and the interaction is well supported; removing the row does not mean it is false. "Protein binding" is uninformative, and the same paper shows GSTU4 is not a camalexin biosynthetic enzyme (camalexin rises in gstu4 knockouts), so no more specific shared function applies. Treated the same way as the CYP71A12 and CYP71A13 protein binding rows that cite PMID:31511315 directly. Supporting Evidence: PMID:31511315 FRET-FLIM and co-IP demonstrated that the glutathione transferase GSTU4, which is coexpressed with Trp- and camalexin-specific enzymes, is physically recruited to the complex.
GO:0005515 protein binding	IPI PMID:33831160 The Formation of a Camalexin Biosynthetic Metabolon.	REMOVE	Summary: IPI with CYP71A12 (AT2G30750). The cited PMID:33831160 is a deleted PubMed duplicate of PMID:31511315 (Mucha et al. 2019), whose co-IP and FRET-FLIM data show the camalexin P450s copurifying with CYP71B15. Reason: This row duplicates the CYP71A12 protein binding row that cites PMID:31511315 directly, which is removed for the same reason. The interaction is real and supports a camalexin metabolon, but "protein binding" says nothing about function; the biology is captured by camalexin biosynthetic process. Supporting Evidence: PMID:31511315 we used two independent untargeted coimmunoprecipitation (co-IP) approaches with the biosynthetic enzymes CYP71B15 and CYP71A13 as baits and determined that the camalexin biosynthetic P450 enzymes copurified with these enzymes.
GO:0005783 endoplasmic reticulum	HDA PMID:16618929 Mapping the Arabidopsis organelle proteome.	ACCEPT	Summary: High-throughput LOPIT organelle proteomics assigning the protein to the ER. Reason: An ER assignment is what is expected for a microsomal P450 with a single N-terminal membrane anchor. It agrees with the enzyme activity recovered in Arabidopsis microsomes and with live-cell imaging of a complementing CYP71B15-GFP fusion in the ER. Supporting Evidence: PMID:16618929 enabling confident and simultaneous localization of 527 proteins to the endoplasmic reticulum, Golgi apparatus, vacuolar membrane, plasma membrane, or mitochondria and plastids PMID:16766671 Arabidopsis microsomes isolated from leaves of CYP71B15-overexpressing and induced wild-type plants were capable of the same reaction but not microsomes from induced leaves of pad3 mutants file:ARATH/CYP71B15/CYP71B15-deep-research-falcon.md Upon fungal challenge, fluorescence appeared mainly in cells adjoining successful infection sites
GO:0005783 endoplasmic reticulum	IDA PMID:33831160 The Formation of a Camalexin Biosynthetic Metabolon.	ACCEPT	Summary: IDA for ER localization. The cited PMID:33831160 is a deleted PubMed duplicate of PMID:31511315 (Mucha et al. 2019, camalexin metabolon), of which only the abstract is available. Reason: The localization imaging in the metabolon paper could not be read (abstract only), but ER localization of PAD3 is independently supported by imaging of a complementing native-promoter CYP71B15-GFP in infected leaves, by LOPIT proteomics, and by microsomal enzyme activity. Accepted, deferring to the curator who read the full text. Supporting Evidence: file:ARATH/CYP71B15/CYP71B15-deep-research-falcon.md Upon fungal challenge, fluorescence appeared mainly in cells adjoining successful infection sites PMID:16766671 Arabidopsis microsomes isolated from leaves of CYP71B15-overexpressing and induced wild-type plants were capable of the same reaction but not microsomes from induced leaves of pad3 mutants
GO:0005788 endoplasmic reticulum lumen	IDA PMID:33831160 The Formation of a Camalexin Biosynthetic Metabolon.	MODIFY	Summary: IDA for ER lumen. The cited PMID:33831160 is a deleted PubMed duplicate of PMID:31511315 (Mucha et al. 2019, camalexin metabolon). Only its abstract is cached; the assay (confocal colocalization with an ER luminal marker) is taken from a full-text reading recorded in the CYP71A13 review. Reason: PAD3 is a type-I microsomal P450 with a single N-terminal membrane anchor (residues 1-21), whose heme domain faces the cytosol where it meets NADPH-P450 reductase, so a luminal location does not fit its topology or chemistry. A full-text reading of the resolved source (Mucha et al. 2019, PMC6881122, recorded in the CYP71A13 and CYP71A12 reviews; not cacheable here) reports that CYP71A12, CYP71A13 and CYP71B15 fusions "were localized to the ER and showed colocalization with the ER lumenal marker RFP-HDEL", and states that eukaryotic P450s are anchored in the ER membrane "with their catalytic centers facing the cytosolic side". Confocal colocalization with a luminal marker shows ER localization but cannot separate lumen from membrane, so the annotation is changed to endoplasmic reticulum membrane, as for CYP71A12 and CYP71A13. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:ARATH/CYP71B15/CYP71B15-uniprot.txt SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane PMID:16766671 Arabidopsis microsomes isolated from leaves of CYP71B15-overexpressing and induced wild-type plants were capable of the same reaction but not microsomes from induced leaves of pad3 mutants
GO:0006952 defense response	IMP PMID:20023151 Tryptophan-derived metabolites are required for antifungal d...	KEEP AS NON CORE	Summary: IMP from genetic epistasis in the mlo2 background: tryptophan-derived metabolites, including camalexin made by PAD3, are needed for mlo2-conditioned antifungal defense. Reason: PAD3 contributes to defense by making camalexin, and pad3 epistasis supports that contribution. "Defense response" is a broad parent of the better-supported, accepted "defense response to fungus". Kept as non-core. Supporting Evidence: PMID:20023151 Results of genetic epistasis analysis suggest a decisive role for indolic metabolites in mlo2-conditioned antifungal defense against both biotrophic powdery mildews and a camalexin-sensitive strain of the necrotrophic fungus Botrytis cinerea.
GO:0006952 defense response	NAS PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	KEEP AS NON CORE	Summary: NAS from the metabolon paper describing camalexin as an antifungal defense compound. Reason: Correct but generic. The specific mechanistic role is camalexin biosynthesis, and the specific physiological role is defense response to fungus. Supporting Evidence: PMID:31511315 efficiently synthesizes the antifungal phytoalexin camalexin without the apparent release of bioactive intermediates
GO:0009414 response to water deprivation	IEP PMID:23144921 Water stress and aphid feeding differentially influence meta...	MARK AS OVER ANNOTATED	Summary: IEP: PAD3 transcript fell about two-fold under drought stress. Reason: A modest drop in transcript level under drought does not show that PAD3 takes part in the response to water deprivation. There is no functional evidence linking camalexin synthesis to drought tolerance. Supporting Evidence: PMID:23144921 Also the transcript level of PAD3 responsible for the final step in camalexin biosynthesis, decreased about two-fold.
GO:0009617 response to bacterium	IEP PMID:17573535 Arabidopsis cytochrome P450 monooxygenase 71A13 catalyzes th...	KEEP AS NON CORE	Summary: IEP: PAD3 expression is induced after infection with Pseudomonas syringae and is co-regulated with CYP71A13. Reason: PAD3 is strongly induced by bacterial infection and camalexin accumulates. Genetically, however, PAD3 is not required for resistance to P. syringae. Kept as a non-core response annotation. Supporting Evidence: PMID:17573535 Expression levels of CYP71A13 and PAD3 are coregulated. PMID:10590168 has no effect on resistance to P. syringae but compromises resistance to the fungal pathogen Alternaria brassicicola
GO:0009617 response to bacterium	IMP PMID:23073694 Metabolic and transcriptomic changes induced in Arabidopsis ...	KEEP AS NON CORE	Summary: IMP: camalexin is needed for the Pseudomonas fluorescens SS101-induced systemic resistance to Pst. Camalexin pathway mutants lost the induced resistance. Reason: The cached abstract lists camalexin pathway mutants but does not name pad3. The curator presumably saw pad3 data in the full text. The finding concerns rhizobacteria-induced resistance, which is an indirect, context-specific role. Kept as non-core. Supporting Evidence: PMID:23073694 showed that camalexin and glucosinolates are indeed required for the induction of Pst resistance by Pf.SS101
GO:0009625 response to insect	IEP PMID:23144921 Water stress and aphid feeding differentially influence meta...	KEEP AS NON CORE	Summary: IEP: aphid feeding (Myzus persicae, Brevicoryne brassicae) up-regulated PAD3 expression. Reason: Induction by aphids fits PAD3 being an inducible defense gene. The cited study shows only expression, so this is kept as non-core. Supporting Evidence: PMID:23144921 Feeding of both, M. persicae and B. brassicae, up-regulated the expression of PAD3 in A. thaliana, but induction was stronger in response to B. brassicae.
GO:0009700 indole phytoalexin biosynthetic process	IMP PMID:8090752 Isolation of phytoalexin-deficient mutants of Arabidopsis th...	ACCEPT	Summary: IMP: the pad3 mutant was isolated in a biochemical screen as phytoalexin deficient. Reason: Correct. Camalexin is the indole phytoalexin of Arabidopsis, and PAD3 catalyses its last steps. The more specific child term, camalexin biosynthetic process, is also annotated. Supporting Evidence: PMID:8090752 A biochemical screen was used to isolate three mutants of A. thaliana ecotype Columbia that were phytoalexin deficient (pad mutants). PMID:16766671 In conclusion, CYP71B15 catalyzes the final step in camalexin biosynthesis.
GO:0009737 response to abscisic acid	IEP PMID:16258012 Transcriptome analysis reveals specific modulation of abscis...	MARK AS OVER ANNOTATED	Summary: IEP from a transcriptome study of ABA responses in rop10 mutants, in which CYP71B15 was among the ABA-responsive genes. Reason: A transcript change in a microarray experiment does not show that PAD3 takes part in the ABA response. No functional link between PAD3 and ABA signalling has been shown. Supporting Evidence: PMID:16258012 This category includes at least a C3HC4-type zinc-finger protein (At5g27420), a putative receptor-like kinase (At3g22060), and a cytochrome P450 (71B15/At3g26830).
GO:0010112 regulation of systemic acquired resistance	IEP PMID:20081042 Arabidopsis auxin mutants are compromised in systemic acquir...	MARK AS OVER ANNOTATED	Summary: IEP from a study of auxin mutants and indolic compounds in systemic acquired resistance (SAR). Reason: Expression evidence cannot support a "regulation of" process term. Even if PAD3 is induced during SAR, induction does not show that it regulates SAR. The abstract implicates indolic compounds in general, not PAD3 or camalexin specifically. Supporting Evidence: PMID:20081042 our data provide compelling evidence for a role of indole-derived compounds, but not auxin itself, in the establishment and maintenance of systemic immunity.
GO:0010120 camalexin biosynthetic process	IDA PMID:16766671 CYP71B15 (PAD3) catalyzes the final step in camalexin biosyn...	ACCEPT	Summary: IDA: recombinant and microsomal CYP71B15 convert dihydrocamalexic acid to camalexin. Reason: Core process. PAD3 catalyses the terminal step(s) of camalexin biosynthesis. Supporting Evidence: PMID:16766671 Recombinant CYP71B15 heterologously expressed in yeast catalyzed the conversion of dihydrocamalexic acid to camalexin with preference of the (S)-enantiomer. PMID:16766671 In conclusion, CYP71B15 catalyzes the final step in camalexin biosynthesis.
GO:0010120 camalexin biosynthetic process	IMP PMID:16766671 CYP71B15 (PAD3) catalyzes the final step in camalexin biosyn...	ACCEPT	Summary: IMP: microsomes from induced pad3 leaves cannot convert DHCA to camalexin, and pad3 accumulates DHCA. Reason: Core process, with direct genetic and biochemical support. Supporting Evidence: PMID:16766671 Arabidopsis microsomes isolated from leaves of CYP71B15-overexpressing and induced wild-type plants were capable of the same reaction but not microsomes from induced leaves of pad3 mutants PMID:16766671 it is now clear that the enhanced susceptibilities of pad3 are the specific results of camalexin deficiency
GO:0010120 camalexin biosynthetic process	NAS PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	ACCEPT	Summary: NAS from the metabolon paper. Reason: Consistent with the experimental annotations. PAD3 is one of the core camalexin biosynthetic P450s. Supporting Evidence: PMID:31511315 we used two independent untargeted coimmunoprecipitation (co-IP) approaches with the biosynthetic enzymes CYP71B15 and CYP71A13 as baits and determined that the camalexin biosynthetic P450 enzymes copurified with these enzymes.
GO:0010298 dihydrocamalexic acid decarboxylase activity	EXP PMID:19567706 The multifunctional enzyme CYP71B15 (PHYTOALEXIN DEFICIENT3)...	ACCEPT	Summary: EXP: yeast-expressed CYP71B15 converts Cys(IAN) to DHCA and then to camalexin. This includes the DHCA-to-camalexin oxidative decarboxylation. Reason: Core molecular function. Note that the GO term is placed under carboxy-lyase activity, and its definition leaves out the O2 and NADPH-P450 reductase the reaction needs; this is raised as a suggested question. It is still the correct and only GO term for the reaction. Supporting Evidence: PMID:19567706 Surprisingly, yeast-expressed CYP71B15 also catalyzed thiazoline ring closure, DHCA formation, and cyanide release with Cys(IAN) as substrate. PMID:19567706 IAN is derivatized to the intermediate Cys(IAN), which serves as substrate of the multifunctional cytochrome P450 enzyme CYP71B15.
GO:0010298 dihydrocamalexic acid decarboxylase activity	IDA PMID:16766671 CYP71B15 (PAD3) catalyzes the final step in camalexin biosyn...	ACCEPT	Summary: IDA: recombinant CYP71B15 in yeast microsomes, and Arabidopsis microsomes, catalyse conversion of DHCA to camalexin. Reason: Core molecular function, demonstrated directly. Supporting Evidence: PMID:16766671 Recombinant CYP71B15 heterologously expressed in yeast catalyzed the conversion of dihydrocamalexic acid to camalexin with preference of the (S)-enantiomer. PMID:16766671 CYP71B15 catalyzes an oxidative decarboxylation of both enantiomers of dihydrocamalexic acid
GO:0010298 dihydrocamalexic acid decarboxylase activity	IEA GO_REF:0000116	ACCEPT	Summary: IEA from the Rhea mapping (RHEA:34807), based on the UniProt catalytic activity annotation. Reason: Matches the experimentally established activity. Supporting Evidence: PMID:16766671 Recombinant CYP71B15 heterologously expressed in yeast catalyzed the conversion of dihydrocamalexic acid to camalexin with preference of the (S)-enantiomer.
GO:0016020 membrane	IEA GO_REF:0000044	MODIFY	Summary: Membrane, mapped from the UniProt subcellular location (single-pass membrane protein). Reason: Correct but uninformative. PAD3 is anchored in the ER by its N-terminal helix (residues 1-21), is recovered in microsomes, and a complementing GFP fusion localizes to the ER. Endoplasmic reticulum membrane is the precise location. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: PMID:16766671 Arabidopsis microsomes isolated from leaves of CYP71B15-overexpressing and induced wild-type plants were capable of the same reaction but not microsomes from induced leaves of pad3 mutants file:ARATH/CYP71B15/CYP71B15-deep-research-falcon.md Upon fungal challenge, fluorescence appeared mainly in cells adjoining successful infection sites
GO:0016020 membrane	NAS PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	MODIFY	Summary: NAS for membrane from the metabolon paper. Reason: As for the IEA membrane row. The metabolon forms at the ER, so endoplasmic reticulum membrane is the informative term. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: PMID:31511315 we used two independent untargeted coimmunoprecipitation (co-IP) approaches with the biosynthetic enzymes CYP71B15 and CYP71A13 as baits and determined that the camalexin biosynthetic P450 enzymes copurified with these enzymes. file:ARATH/CYP71B15/CYP71B15-deep-research-falcon.md Upon fungal challenge, fluorescence appeared mainly in cells adjoining successful infection sites
GO:0016491 oxidoreductase activity	IBA GO_REF:0000033	ACCEPT	Summary: IBA: oxidoreductase activity propagated from a PANTHER CYP71 node. Reason: Correct at the family level. Both PAD3 reactions are O2- and reductase-dependent oxidations (EC 1.14.19.52). PAD3 lies inside the CYP71 clade, and there is no evidence that it has lost the activity. Supporting Evidence: PMID:16766671 CYP71B15 catalyzes an oxidative decarboxylation of both enantiomers of dihydrocamalexic acid PMID:19567706 Surprisingly, yeast-expressed CYP71B15 also catalyzed thiazoline ring closure, DHCA formation, and cyanide release with Cys(IAN) as substrate.
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen	IEA GO_REF:0000002	ACCEPT	Summary: InterPro mapping to oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen. Reason: Accurate grouping term for both characterised reactions. EC 1.14.19.52 lies in the EC 1.14.19 class, where the paired donors are oxidized and O2 is reduced to water. This fits better than monooxygenase activity. Supporting Evidence: PMID:16766671 CYP71B15 catalyzes an oxidative decarboxylation of both enantiomers of dihydrocamalexic acid PMID:19567706 Surprisingly, yeast-expressed CYP71B15 also catalyzed thiazoline ring closure, DHCA formation, and cyanide release with Cys(IAN) as substrate.
GO:0020037 heme binding	IEA GO_REF:0000002	ACCEPT	Summary: InterPro mapping to heme binding (cytochrome P450 domain with the heme-binding cysteine signature). Reason: The heme-thiolate cofactor is required for P450 catalysis. PAD3 has the P450 heme-binding cysteine signature (IPR017972). Supporting Evidence: PMID:10590168 The predicted PAD3 protein appears to be a cytochrome P450 monooxygenase, similar to those from maize
GO:0050832 defense response to fungus	IMP PMID:26813622 Pectin Biosynthesis Is Critical for Cell Wall Integrity and ...	ACCEPT	Summary: IMP: pad3 mutants are more susceptible to necrotrophic fungi. Reason: pad3 is markedly more susceptible to Alternaria brassicicola, and depending on the isolate to Botrytis cinerea. Because PAD3 itself makes the antifungal phytoalexin, its role in fungal defense is a direct, enzymatic contribution, not an indirect regulatory one. This is the physiological role of the camalexin biosynthetic activity. Supporting Evidence: PMID:10476063 We now show that this mutant is markedly more susceptible than its wild-type parental line to infection by the necrotrophic fungus Alternaria brassicicola, but not to Botrytis cinerea. PMID:12848825 The rate of development of B. cinerea disease symptoms on primary infected leaves was affected by responses mediated by the genes EIN2, JAR1, EDS4, PAD2, and PAD3 PMID:12848825 camalexin limits lesion development PMID:16766671 it is now clear that the enhanced susceptibilities of pad3 are the specific results of camalexin deficiency
GO:1902494 catalytic complex	NAS PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	KEEP AS NON CORE	Summary: NAS: PAD3 as part of the camalexin biosynthetic metabolon. Reason: PAD3 associates with CYP71A12, CYP71A13, CYP79B2 and GSTU4 in an ER-associated assembly. This looks like a dynamic metabolon rather than a stable complex of defined composition, and PAD3 has its catalytic activity on its own (recombinant enzyme in yeast). "Catalytic complex" is acceptable as a vague description but is not core. Supporting Evidence: PMID:31511315 we used two independent untargeted coimmunoprecipitation (co-IP) approaches with the biosynthetic enzymes CYP71B15 and CYP71A13 as baits and determined that the camalexin biosynthetic P450 enzymes copurified with these enzymes. PMID:16766671 Recombinant CYP71B15 heterologously expressed in yeast catalyzed the conversion of dihydrocamalexic acid to camalexin with preference of the (S)-enantiomer.

Gene Description

Proposed New Ontology Terms

dihydrocamalexate synthase activity

Existing Annotations Review

Core Functions

Oxidative decarboxylation of (R/S)-dihydrocamalexic acid to camalexin, the final step of camalexin biosynthesis, at the ER membrane.

Conversion of the cysteine-indole-3-acetonitrile conjugate Cys(IAN) to dihydrocamalexic acid, with thiazoline ring closure and cyanide release (RHEA:10452). GO has no term for this reaction yet.

Camalexin produced by PAD3 is an antifungal phytoalexin required for resistance to necrotrophic fungi such as Alternaria brassicicola and Botrytis cinerea.

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

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