BCAT2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003824 catalytic activity	IEA GO_REF:0000002	MODIFY	Summary: Branched-chain-amino-acid transamination is the established catalytic reaction. Reason: Branched-chain-amino-acid transamination is the established catalytic reaction. This assessment transfers characterized mammalian biology to the selected horse sequence with the sequence limitations stated in the comparison. Proposed replacements: branched-chain-amino-acid:2-oxoglutarate transaminase activity Supporting Evidence: file:human/BCAT2/BCAT2-uniprot.txt CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the CC essential branched chain amino acids leucine, isoleucine, and valine CC (PubMed:17050531, PubMed:25653144, PubMed:8702755). Branched chain CC amino acid catabolism plays a role in adipocyte differentiation by CC providing lipogenic acetyl-CoA pools in differentiated adipocytes (By CC similarity). Mechanistically, acetyl-CoA derived from branched chain CC amino acid catabolism is used by EP300/p300 to acetylate and inhibit CC PRDM16, thereby preventing adipose tissue browning (By similarity). May CC also function as a transporter of branched chain alpha-keto acids (By CC similarity). {ECO:0000250\|UniProtKB:O35854, CC ECO:0000250\|UniProtKB:O35855, ECO:0000269\|PubMed:17050531, CC ECO:0000269\|PubMed:25653144, ECO:0000269\|PubMed:8702755}. file:HORSE/BCAT2/BCAT2-bioinformatics/RESULTS.md The horse sequence A0A9L0TSN4 (452 residues) aligns to human O15382 (392 residues) with 83.42% identity across 392 paired residues. Paired coverage is 100.0% of the human sequence and 86.73% of the horse sequence. PMID:17050531 Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-Ox) have been used to elucidate the role of this center in hBCATm catalysis. X-ray crystallography revealed that the CXXC motif, through its network of hydrogen bonds, plays a crucial role in orienting the substrate optimally for catalysis. In all structures, there were changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein.
GO:0004084 branched-chain-amino-acid:2-oxoglutarate transaminase activity	IEA GO_REF:0000120	ACCEPT	Summary: Human BCAT2 structural/kinetic studies establish branched-chain amino acid transamination; the horse protein conserves mapped substrate contacts throughout the full human enzyme. Reason: Human BCAT2 structural/kinetic studies establish branched-chain amino acid transamination; the horse protein conserves mapped substrate contacts throughout the full human enzyme. This assessment transfers characterized mammalian biology to the selected horse sequence with the sequence limitations stated in the comparison. Supporting Evidence: file:human/BCAT2/BCAT2-uniprot.txt CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the CC essential branched chain amino acids leucine, isoleucine, and valine CC (PubMed:17050531, PubMed:25653144, PubMed:8702755). Branched chain CC amino acid catabolism plays a role in adipocyte differentiation by CC providing lipogenic acetyl-CoA pools in differentiated adipocytes (By CC similarity). Mechanistically, acetyl-CoA derived from branched chain CC amino acid catabolism is used by EP300/p300 to acetylate and inhibit CC PRDM16, thereby preventing adipose tissue browning (By similarity). May CC also function as a transporter of branched chain alpha-keto acids (By CC similarity). {ECO:0000250\|UniProtKB:O35854, CC ECO:0000250\|UniProtKB:O35855, ECO:0000269\|PubMed:17050531, CC ECO:0000269\|PubMed:25653144, ECO:0000269\|PubMed:8702755}. file:HORSE/BCAT2/BCAT2-bioinformatics/RESULTS.md The horse sequence A0A9L0TSN4 (452 residues) aligns to human O15382 (392 residues) with 83.42% identity across 392 paired residues. Paired coverage is 100.0% of the human sequence and 86.73% of the horse sequence. PMID:17050531 Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-Ox) have been used to elucidate the role of this center in hBCATm catalysis. X-ray crystallography revealed that the CXXC motif, through its network of hydrogen bonds, plays a crucial role in orienting the substrate optimally for catalysis. In all structures, there were changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein.
GO:0005739 mitochondrion	IEA GO_REF:0000044	UNDECIDED	Summary: The selected horse model has a 60-residue N-terminal extension. Conservation of the mature enzyme supports catalysis but does not verify processing or mitochondrial targeting of this particular N terminus. Reason: The selected horse model has a 60-residue N-terminal extension. Conservation of the mature enzyme supports catalysis but does not verify processing or mitochondrial targeting of this particular N terminus. This assessment transfers characterized mammalian biology to the selected horse sequence with the sequence limitations stated in the comparison. Supporting Evidence: file:human/BCAT2/BCAT2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250\|UniProtKB:O35854}. file:HORSE/BCAT2/BCAT2-bioinformatics/RESULTS.md The horse sequence A0A9L0TSN4 (452 residues) aligns to human O15382 (392 residues) with 83.42% identity across 392 paired residues. Paired coverage is 100.0% of the human sequence and 86.73% of the horse sequence.
GO:0009081 branched-chain amino acid metabolic process	IEA GO_REF:0000002	MODIFY	Summary: The characterized role is branched-chain amino acid catabolism. Reason: The characterized role is branched-chain amino acid catabolism. This assessment transfers characterized mammalian biology to the selected horse sequence with the sequence limitations stated in the comparison. Proposed replacements: branched-chain amino acid catabolic process Supporting Evidence: file:human/BCAT2/BCAT2-uniprot.txt CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the CC essential branched chain amino acids leucine, isoleucine, and valine CC (PubMed:17050531, PubMed:25653144, PubMed:8702755). Branched chain CC amino acid catabolism plays a role in adipocyte differentiation by CC providing lipogenic acetyl-CoA pools in differentiated adipocytes (By CC similarity). Mechanistically, acetyl-CoA derived from branched chain CC amino acid catabolism is used by EP300/p300 to acetylate and inhibit CC PRDM16, thereby preventing adipose tissue browning (By similarity). May CC also function as a transporter of branched chain alpha-keto acids (By CC similarity). {ECO:0000250\|UniProtKB:O35854, CC ECO:0000250\|UniProtKB:O35855, ECO:0000269\|PubMed:17050531, CC ECO:0000269\|PubMed:25653144, ECO:0000269\|PubMed:8702755}. file:HORSE/BCAT2/BCAT2-bioinformatics/RESULTS.md The horse sequence A0A9L0TSN4 (452 residues) aligns to human O15382 (392 residues) with 83.42% identity across 392 paired residues. Paired coverage is 100.0% of the human sequence and 86.73% of the horse sequence. PMID:17050531 Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-Ox) have been used to elucidate the role of this center in hBCATm catalysis. X-ray crystallography revealed that the CXXC motif, through its network of hydrogen bonds, plays a crucial role in orienting the substrate optimally for catalysis. In all structures, there were changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein.
GO:0009083 branched-chain amino acid catabolic process	IEA GO_REF:0000117	ACCEPT	Summary: The conserved enzyme catalyzes the first transamination step in branched-chain amino acid breakdown. Reason: The conserved enzyme catalyzes the first transamination step in branched-chain amino acid breakdown. This assessment transfers characterized mammalian biology to the selected horse sequence with the sequence limitations stated in the comparison. Supporting Evidence: file:human/BCAT2/BCAT2-uniprot.txt CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the CC essential branched chain amino acids leucine, isoleucine, and valine CC (PubMed:17050531, PubMed:25653144, PubMed:8702755). Branched chain CC amino acid catabolism plays a role in adipocyte differentiation by CC providing lipogenic acetyl-CoA pools in differentiated adipocytes (By CC similarity). Mechanistically, acetyl-CoA derived from branched chain CC amino acid catabolism is used by EP300/p300 to acetylate and inhibit CC PRDM16, thereby preventing adipose tissue browning (By similarity). May CC also function as a transporter of branched chain alpha-keto acids (By CC similarity). {ECO:0000250\|UniProtKB:O35854, CC ECO:0000250\|UniProtKB:O35855, ECO:0000269\|PubMed:17050531, CC ECO:0000269\|PubMed:25653144, ECO:0000269\|PubMed:8702755}. file:HORSE/BCAT2/BCAT2-bioinformatics/RESULTS.md The horse sequence A0A9L0TSN4 (452 residues) aligns to human O15382 (392 residues) with 83.42% identity across 392 paired residues. Paired coverage is 100.0% of the human sequence and 86.73% of the horse sequence. PMID:17050531 Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-Ox) have been used to elucidate the role of this center in hBCATm catalysis. X-ray crystallography revealed that the CXXC motif, through its network of hydrogen bonds, plays a crucial role in orienting the substrate optimally for catalysis. In all structures, there were changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein.

Core Functions

BCAT2 is a branched-chain-amino-acid aminotransferase that initiates leucine, isoleucine and valine catabolism. The selected horse protein conserves the human catalytic and substrate-binding architecture but carries an additional N-terminal segment whose effect on mitochondrial targeting is unresolved.

Molecular Function:

branched-chain-amino-acid:2-oxoglutarate transaminase activity

Supporting Evidence:

file:human/BCAT2/BCAT2-uniprot.txt
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the CC essential branched chain amino acids leucine, isoleucine, and valine CC (PubMed:17050531, PubMed:25653144, PubMed:8702755). Branched chain CC amino acid catabolism plays a role in adipocyte differentiation by CC providing lipogenic acetyl-CoA pools in differentiated adipocytes (By CC similarity). Mechanistically, acetyl-CoA derived from branched chain CC amino acid catabolism is used by EP300/p300 to acetylate and inhibit CC PRDM16, thereby preventing adipose tissue browning (By similarity). May CC also function as a transporter of branched chain alpha-keto acids (By CC similarity). {ECO:0000250|UniProtKB:O35854, CC ECO:0000250|UniProtKB:O35855, ECO:0000269|PubMed:17050531, CC ECO:0000269|PubMed:25653144, ECO:0000269|PubMed:8702755}.
file:HORSE/BCAT2/BCAT2-bioinformatics/RESULTS.md
The horse sequence A0A9L0TSN4 (452 residues) aligns to human O15382 (392 residues) with 83.42% identity across 392 paired residues. Paired coverage is 100.0% of the human sequence and 86.73% of the horse sequence.
PMID:17050531
Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-Ox) have been used to elucidate the role of this center in hBCATm catalysis. X-ray crystallography revealed that the CXXC motif, through its network of hydrogen bonds, plays a crucial role in orienting the substrate optimally for catalysis. In all structures, there were changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein.

Gene Description

Existing Annotations Review

Core Functions

References

📚 Additional Documentation

Notes

Bioinformatics Results

Protnlm Function Review

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