D00106
type: Enzyme
rlcp: p5300
rlcp: p5520
cath: D-amino Acid Aminotransferase; Chain A, domain 1
cath: D-amino Acid Aminotransferase; Chain A, domain 2
ec: https://purl.uniprot.org/enzyme/2.6.1.42
csa: 1iyd
uniprot: P0AB80
uniprot: O15382
kegg enzyme: branched-chain-amino-acid transaminase
kegg pathway: Valine, leucine and isoleucine degradation
kegg pathway: Valine, leucine and isoleucine biosynthesis
kegg pathway: Pantothenate and CoA biosynthesis
kegg cofactor: Pyridoxal phosphate
kegg substrate: L-Leucine
kegg substrate: L-Isoleucine
kegg substrate: L-Valine
kegg substrate: 2-Oxoglutarate
kegg product: 4-Methyl-2-oxopentanoate
kegg product: 3-Methyl-2-oxopentanoate
kegg product: 3-Methyl-2-oxobutanoate
kegg product: L-Glutamate
pdb: 1a3gA01
pdb: 1a3gB01
pdb: 1a3gC01
pdb: 1i1kA01
pdb: 1i1kB01
pdb: 1i1kC01
pdb: 1i1lA01
pdb: 1i1lB01
pdb: 1i1lC01
pdb: 1i1mA01
pdb: 1i1mB01
pdb: 1i1mC01
pdb: 1iydA01
pdb: 1iydB01
pdb: 1iydC01
pdb: 1iyeA01
pdb: 1iyeB01
pdb: 1iyeC01
pdb: 1ekfA01
pdb: 1ekfB01
pdb: 1ekpA01
pdb: 1ekpB01
pdb: 1ekvA01
pdb: 1ekvB01
pdb: 1kt8A01
pdb: 1kt8B01
pdb: 1ktaA01
pdb: 1ktaB01
pdb: 1a3gA02
pdb: 1a3gB02
pdb: 1a3gC02
pdb: 1i1kA02
pdb: 1i1kB02
pdb: 1i1kC02
pdb: 1i1lA02
pdb: 1i1lB02
pdb: 1i1lC02
pdb: 1i1mA02
pdb: 1i1mB02
pdb: 1i1mC02
pdb: 1iydA02
pdb: 1iydB02
pdb: 1iydC02
pdb: 1iyeA02
pdb: 1iyeB02
pdb: 1iyeC02
pdb: 1ekfA02
pdb: 1ekfB02
pdb: 1ekpA02
pdb: 1ekpB02
pdb: 1ekvA02
pdb: 1ekvB02
pdb: 1kt8A02
pdb: 1kt8B02
pdb: 1ktaA02
pdb: 1ktaB02
references: Crystallization and preliminary X-ray characterization of branched-chain amino acid aminotransferase from Escherichia coli.
references: Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution.

D-amino Acid Aminotransferase; Chain A, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.470.10

D-amino Acid Aminotransferase; Chain A, domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.10.10
catalytic domain: index.html

Valine, leucine and isoleucine degradation
type: KeggPathway
references: KEGG:MAP00280

Valine, leucine and isoleucine biosynthesis
type: KeggPathway
references: KEGG:MAP00290

Pantothenate and CoA biosynthesis
type: KeggPathway
references: KEGG:MAP00770

Pyridoxal phosphate
type: KeggCofactor
references: KEGG:C00018
compound type: aromatic ring (with nitrogen atoms)
compound type: phosphate group/phosphate ion
references: CHEBI:18405
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Leucine
type: KeggSubstrate
references: KEGG:C00123
compound type: amino acids
references: CHEBI:15603
references: CHEBI:57427
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Isoleucine
type: KeggSubstrate
references: KEGG:C00407
compound type: amino acids
references: CHEBI:17191
references: CHEBI:58045
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Valine
type: KeggSubstrate
references: KEGG:C00183
compound type: amino acids
references: CHEBI:16414
references: CHEBI:57762
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

2-Oxoglutarate
type: KeggSubstrate
references: KEGG:C00026
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:30915
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

4-Methyl-2-oxopentanoate
type: KeggProduct
references: KEGG:C00233
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:48430
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

3-Methyl-2-oxopentanoate
type: KeggProduct
references: KEGG:C03465
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:35932
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

3-Methyl-2-oxobutanoate
type: KeggProduct
references: KEGG:C00141
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:16530
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Glutamate
type: KeggProduct
references: KEGG:C00025
compound type: amino acids
compound type: carboxyl group
references: CHEBI:16015
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1a3gA02
type: Pdb
references: 1a3g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3g
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1a3gB02
type: Pdb
references: 1a3g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3g
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1a3gC02
type: Pdb
references: 1a3g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3g
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1i1kA02
type: Pdb
references: 1i1k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1k
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1i1kB02
type: Pdb
references: 1i1k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1k
catalytic residue: LYS 659;TYR 664
cofactor binding residue: LYS 659(PLP binding)

1i1kC02
type: Pdb
references: 1i1k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1k
catalytic residue: LYS 1159;TYR 1164
cofactor binding residue: LYS 1159(PLP binding)

1i1lA02
type: Pdb
references: 1i1l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1l
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1i1lB02
type: Pdb
references: 1i1l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1l
catalytic residue: LYS 659;TYR 664
cofactor binding residue: LYS 659(PLP binding)

1i1lC02
type: Pdb
references: 1i1l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1l
catalytic residue: LYS 1159;TYR 1164
cofactor binding residue: LYS 1159(PLP binding)

1i1mA02
type: Pdb
references: 1i1m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1m
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1i1mB02
type: Pdb
references: 1i1m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1m
catalytic residue: LYS 659;TYR 664
cofactor binding residue: LYS 659(PLP binding)

1i1mC02
type: Pdb
references: 1i1m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i1m
catalytic residue: LYS 1159;TYR 1164
cofactor binding residue: LYS 1159(PLP binding)

1iydA02
type: Pdb
references: 1iyd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iyd
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1iydB02
type: Pdb
references: 1iyd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iyd
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1iydC02
type: Pdb
references: 1iyd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iyd
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1iyeA02
type: Pdb
references: 1iye
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iye
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1iyeB02
type: Pdb
references: 1iye
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iye
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1iyeC02
type: Pdb
references: 1iye
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iye
catalytic residue: LYS 159;TYR 164
cofactor binding residue: LYS 159(PLP binding)

1ekfA02
type: Pdb
references: 1ekf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ekf
catalytic residue: LYS 202;TYR 207
cofactor binding residue: LYS 202(PLP binding)

1ekfB02
type: Pdb
references: 1ekf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ekf
catalytic residue: LYS 202;TYR 207
cofactor binding residue: LYS 202(PLP binding)

1ekpA02
type: Pdb
references: 1ekp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ekp
catalytic residue: LYS 202;TYR 207
cofactor binding residue: LYS 202(PLP binding)

1ekpB02
type: Pdb
references: 1ekp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ekp
catalytic residue: LYS 202;TYR 207
cofactor binding residue: LYS 202(PLP binding)

1ekvA02
type: Pdb
references: 1ekv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ekv
catalytic residue: LYS 202;TYR 207
cofactor binding residue: LYS 202(PLP binding)

1ekvB02
type: Pdb
references: 1ekv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ekv
catalytic residue: LYS 202;TYR 207
cofactor binding residue: LYS 202(PLP binding)

1kt8A02
type: Pdb
references: 1kt8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kt8
catalytic residue: LYS 202;TYR 207
cofactor binding residue: LYS 202(PLP binding)

1kt8B02
type: Pdb
references: 1kt8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kt8
catalytic residue: LYS 702;TYR 707
cofactor binding residue: LYS 702(PLP binding)

1ktaA02
type: Pdb
references: 1kta
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kta
catalytic residue: LYS 202;TYR 207
cofactor binding residue: LYS 202(PLP binding)

1ktaB02
type: Pdb
references: 1kta
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kta
catalytic residue: LYS 702;TYR 707
cofactor binding residue: LYS 702(PLP binding)

Crystallization and preliminary X-ray characterization of branched-chain amino acid aminotransferase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2666406
journal: J Biochem (Tokyo)
volume: 105
pages: 671-2
published year: 1989
authors:
  item: Kamitori S
  item: Odagaki Y
  item: Inoue K
  item: Kuramitsu S
  item: Kagamiyama H
  item: Matsuura Y
  item: Higuchi T

Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
medline id: 97306043
references: http://www.ncbi.nlm.nih.gov/pubmed/9163511
journal: J Biochem (Tokyo)
volume: 121
pages: 637-41
published year: 1997
authors:
  item: Okada K
  item: Hirotsu K
  item: Sato M
  item: Hayashi H
  item: Kagamiyama H
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AB80

Structure, evolution and action of vitamin B6-dependent enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9914259
journal: Curr Opin Struct Biol
volume: 8
pages: 759-69
published year: 1998
authors:
  item: Jansonius JN

Branched-chain amino-acid aminotransferase of Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10989422
journal: Methods Enzymol
volume: 324
pages: 103-13
published year: 2000
authors:
  item: Kagamiyama H
  item: Hayashi H

The structure of human mitochondrial branched-chain aminotransferase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11264579
journal: Acta Crystallogr D Biol Crystallogr
volume: 57
pages: 506-15
published year: 2001
authors:
  item: Yennawar N
  item: Dunbar J
  item: Conway M
  item: Hutson S
  item: Farber G
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11412098
journal: Biochemistry
volume: 40
pages: 7453-63
published year: 2001
authors:
  item: Okada K
  item: Hirotsu K
  item: Hayashi H
  item: Kagamiyama H
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure and function of branched chain aminotransferases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11642362
journal: Prog Nucleic Acid Res Mol Biol
volume: 70
pages: 175-206
published year: 2001
authors:
  item: Hutson S

Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12119021
journal: Biochemistry
volume: 41
pages: 9070-8
published year: 2002
authors:
  item: Conway ME
  item: Yennawar N
  item: Wallin R
  item: Poole LB
  item: Hutson SM

Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12269802
journal: Biochemistry
volume: 41
pages: 11592-601
published year: 2002
authors:
  item: Yennawar NH
  item: Conway ME
  item: Yennawar HP
  item: Farber GK
  item: Hutson SM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12667063
journal: Biochemistry
volume: 42
pages: 3725-33
published year: 2003
authors:
  item: Goto M
  item: Miyahara I
  item: Hayashi H
  item: Kagamiyama H
  item: Hirotsu K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

transaminase B
type: KeggEnzyme

branched-chain amino acid aminotransferase
type: KeggEnzyme

branched-chain amino acid-glutamate transaminase
type: KeggEnzyme

branched-chain aminotransferase
type: KeggEnzyme

L-branched chain amino acid aminotransferase
type: KeggEnzyme

glutamate-branched-chain amino acid transaminase
type: KeggEnzyme

Analogue
compound: L-Valine
pdb: 1i1mA02
ligand het code: 4MV

Analogue
compound: L-Valine
pdb: 1i1mB02
ligand het code: 4MV

Analogue
compound: L-Valine
pdb: 1i1mC02
ligand het code: 4MV

Analogue
compound: 2-Oxoglutarate
pdb: 1iydA01
ligand het code: GUA

Analogue
compound: 2-Oxoglutarate
pdb: 1iydB01
ligand het code: GUA

Analogue
compound: 2-Oxoglutarate
pdb: 1iydC01
ligand het code: GUA

Analogue
compound: 2-Oxoglutarate
pdb: 1ktaA02
ligand het code: KIV

Analogue
compound: Pyridoxal phosphate
pdb: 1iyeA02
ligand het code: PGU

Analogue
compound: Pyridoxal phosphate
pdb: 1iyeB02
ligand het code: PGU

Analogue
compound: Pyridoxal phosphate
pdb: 1iyeC02
ligand het code: PGU

Analogue
compound: Pyridoxal phosphate
pdb: 1kt8A02
ligand het code: ILP

Analogue
compound: Pyridoxal phosphate
pdb: 1kt8B02
ligand het code: ILP

Analogue
compound: Pyridoxal phosphate
pdb: 1ktaA02
ligand het code: PMP

Analogue
compound: Pyridoxal phosphate
pdb: 1ktaB02
ligand het code: PMP

IntermediateAnalogue
pdb: 1i1lA02
ligand het code: PLP-2ML

IntermediateAnalogue
pdb: 1i1lB02
ligand het code: PLP-2ML

IntermediateAnalogue
pdb: 1i1lC02
ligand het code: PLP-2ML

IntermediateAnalogue
pdb: 1iyeA02
ligand het code: PGU

IntermediateAnalogue
pdb: 1iyeB02
ligand het code: PGU

IntermediateAnalogue
pdb: 1iyeC02
ligand het code: PGU

IntermediateBound
pdb: 1kt8A02
ligand het code: ILP

IntermediateBound
pdb: 1kt8B02
ligand het code: ILP

IntermediateAnalogue
pdb: 1ekvA02
ligand het code: PLP-TRS

IntermediateAnalogue
pdb: 1ekvB02
ligand het code: PLP-TRS

ReferenceForCatalyticMechanism
reference index: 5
reference section: p.111-112

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.7459-7460

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.11594-11599

ReferenceForCatalyticMechanism
reference index: 10
reference section: Scheme 2, Fig.7, p.3728-3730, p.3731-3733