T00011
type: Enzyme
active site residues resources: P00366
cath: Helix Hairpins
cath: Leucine Dehydrogenase; Chain A, domain 1
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.4.1.3
kegg enzyme: glutamate dehydrogenase [NAD(P)+]
kegg pathway: Glutamate metabolism
kegg pathway: Arginine and proline metabolism
kegg pathway: D-Glutamine and D-glutamate metabolism
kegg pathway: Nitrogen metabolism
kegg product: 2-Oxoglutarate
kegg product: NH3
kegg product: H+
kegg product: NADH
kegg product: NADPH
kegg substrate: L-Glutamate
kegg substrate: H2O
kegg substrate: NAD+
kegg substrate: NADP+
pdb: 1ch6A03
pdb: 1ch6B03
pdb: 1ch6C03
pdb: 1ch6D03
pdb: 1ch6E03
pdb: 1ch6F03
pdb: 1hwxA01
pdb: 1hwxB01
pdb: 1hwxC01
pdb: 1hwxD01
pdb: 1hwxE01
pdb: 1hwxF01
pdb: 1hwyA01
pdb: 1hwyB01
pdb: 1hwyC01
pdb: 1hwyD01
pdb: 1hwyE01
pdb: 1hwyF01
pdb: 1hwzA01
pdb: 1hwzB01
pdb: 1hwzC01
pdb: 1hwzD01
pdb: 1hwzE01
pdb: 1hwzF01
pdb: 1ch6A01
pdb: 1ch6B01
pdb: 1ch6C01
pdb: 1ch6D01
pdb: 1ch6E01
pdb: 1ch6F01
pdb: 1hwxA02
pdb: 1hwxB02
pdb: 1hwxC02
pdb: 1hwxD02
pdb: 1hwxE02
pdb: 1hwxF02
pdb: 1hwyA02
pdb: 1hwyB02
pdb: 1hwyC02
pdb: 1hwyD02
pdb: 1hwyE02
pdb: 1hwyF02
pdb: 1hwzA02
pdb: 1hwzB02
pdb: 1hwzC02
pdb: 1hwzD02
pdb: 1hwzE02
pdb: 1hwzF02
pdb: 1ch6A02
pdb: 1ch6B02
pdb: 1ch6C02
pdb: 1ch6D02
pdb: 1ch6E02
pdb: 1ch6F02
pdb: 1hwxA03
pdb: 1hwxB03
pdb: 1hwxC03
pdb: 1hwxD03
pdb: 1hwxE03
pdb: 1hwxF03

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.4, p.884
reference step: 3

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.2749-2751

ReferenceForCatalyticMechanism
reference index: 19
reference section: p.714

Helix Hairpins
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.287.140

Leucine Dehydrogenase; Chain A, domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.192.10

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720

H2O
type: KeggSubstrate
compound type: H2O
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggProduct
compound type: others
references: KEGG:C00080
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Glutamate metabolism
type: KeggPathway
references: KEGG:MAP00251

Arginine and proline metabolism
type: KeggPathway
references: KEGG:MAP00330

D-Glutamine and D-glutamate metabolism
type: KeggPathway
references: KEGG:MAP00471

Nitrogen metabolism
type: KeggPathway
references: KEGG:MAP00910

Studies of glutamate dehydrogenase: chemical modification and quantitative determination of tryptophan residues.
type: BibliographicResource
authors:
  item: Witzemann V
  item: Koberstein R
  item: Sund H
  item: Rasched I
  item: Jornvall H
  item: Noack K
journal: Eur J Biochem
medline id: 74252258
pages: 319-25
published year: 1974
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/4365183
references: P00366
comment: CHARACTERIZATION.

The demonstration of a glutamate dehydrogenase-NADP-L-glutamate charge-transfer complex and its location on the reaction pathway.
type: BibliographicResource
authors:
  item: Saha SK
  item: Maniscalco SJ
  item: Singh N
  item: Fisher HF
journal: J Biol Chem
pages: 29592-7
published year: 1994
volume: 269
references: http://www.ncbi.nlm.nih.gov/pubmed/7961946

Crystallization and characterization of bovine liver glutamate dehydrogenase.
type: BibliographicResource
authors:
  item: Peterson PE
  item: Pierce J
  item: Smith TJ
journal: J Struct Biol
pages: 73-7
published year: 1997
volume: 120
references: http://www.ncbi.nlm.nih.gov/pubmed/9356294

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00011#12
type: BibliographicResource
title: Identification and characterization of kinetically competent carbinolamine and alpha-iminoglutarate complexes in the glutamate dehydrogenase-catalyzed oxidation of L-glutamate using a multiwavelength transient state approach.
authors:
  item: Maniscalco SJ
  item: Saha SK
  item: Fisher HF
journal: Biochemistry
pages: 14585-90
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9772187

Photoaffinity labeling of brain glutamate dehydrogenase isoproteins with an azido-ADP.
type: BibliographicResource
authors:
  item: Cho SW
  item: Yoon HY
journal: J Biol Chem
pages: 13948-53
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/10318805

The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery.
type: BibliographicResource
authors:
  item: Peterson PE
  item: Smith TJ
journal: Structure Fold Des
medline id: 99354411
pages: 769-82
published year: 1999
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/10425679
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00366
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Stabilization of noncovalent intermediates in enzymatically catalyzed reactions.
type: BibliographicResource
authors:
  item: Fisher HF
  item: Maniscalco SJ
  item: Tally J
journal: Biochem Biophys Res Commun
pages: 343-7
published year: 2001
volume: 287
references: http://www.ncbi.nlm.nih.gov/pubmed/11554732

Adenosine 5'-0-[S-(4-succinimidyl-benzophenone)thiophosphate]: a new photoaffinity label of the allosteric ADP site of bovine liver glutamate dehydrogenase.
type: BibliographicResource
authors:
  item: Madhusoodanan KS
  item: Colman RF
journal: Biochemistry
pages: 1577-86
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11327816

Cassette mutagenesis of lysine 130 of human glutamate dehydrogenase. An essential residue in catalysis.
type: BibliographicResource
authors:
  item: Cho SW
  item: Yoon HY
  item: Ahn JY
  item: Lee EY
  item: Lee J
journal: Eur J Biochem
pages: 3205-13
published year: 2001
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/11389722

Octyl glucoside induced formation of the molten globule-like state of glutamate dehydrogenase.
type: BibliographicResource
authors:
  item: Ghobadi S
  item: Safarian S
  item: Moosavi-Movahedi AA
  item: Ranjbar B
journal: J Biochem (Tokyo)
pages: 671-7
published year: 2001
volume: 130
references: http://www.ncbi.nlm.nih.gov/pubmed/11686930

Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation.
type: BibliographicResource
authors:
  item: Smith TJ
  item: Peterson PE
  item: Schmidt T
  item: Fang J
  item: Stanley CA
journal: J Mol Biol
pages: 707-20
published year: 2001
volume: 307
references: http://www.ncbi.nlm.nih.gov/pubmed/11254391
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

L-Glutamic acid dehydrogenase.
type: BibliographicResource
authors:
  item: Gore MG
journal: Int J Biochem
pages: 879-86
published year: 1981
volume: 13
references: http://www.ncbi.nlm.nih.gov/pubmed/7024012

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00011#20
type: BibliographicResource
title: Substitution of Ser for Arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and L-leucine.
authors:
  item: Zaganas I
  item: Spanaki C
  item: Karpusas M
  item: Plaitakis A
journal: J Biol Chem
pages: 46552-8
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/12324473

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00011#21
type: BibliographicResource
title: Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme.
authors:
  item: Zaganas I
  item: Plaitakis A
journal: J Biol Chem
pages: 26422-8
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11950837

The structure of apo human glutamate dehydrogenase details subunit communication and allostery.
type: BibliographicResource
authors:
  item: Smith TJ
  item: Schmidt T
  item: Fang J
  item: Wu J
  item: Siuzdak G
  item: Stanley CA
journal: J Mol Biol
pages: 765-77
published year: 2002
volume: 318
references: http://www.ncbi.nlm.nih.gov/pubmed/12054821
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Catalytic activity of bovine glutamate dehydrogenase requires a hexamer structure.
type: BibliographicResource
authors:
  item: Bell ET
  item: Bell JE
journal: Biochem J
pages: 327-30
published year: 1984
volume: 217
references: http://www.ncbi.nlm.nih.gov/pubmed/6696727

Carbonyl oxygen exchange evidence of imine formation in the glutamate dehydrogenase reaction and identification of the "occult role" of NADPH.
type: BibliographicResource
authors:
  item: Fisher HF
  item: Viswanathan TS
journal: Proc Natl Acad Sci U S A
pages: 2747-51
published year: 1984
volume: 81
references: http://www.ncbi.nlm.nih.gov/pubmed/6144102

A transfer nuclear Overhauser effect study of coenzyme binding to distinct sites in binary and ternary complexes in glutamate dehydrogenase.
type: BibliographicResource
authors:
  item: Banerjee A
  item: Levy HR
  item: Levy GC
  item: LiMuti C
  item: Goldstein BM
  item: Bell JE
journal: Biochemistry
pages: 8443-50
published year: 1987
volume: 26
references: http://www.ncbi.nlm.nih.gov/pubmed/3442667

Reversible association of ox liver glutamate dehydrogenase with the inner mitochondrial membrane.
type: BibliographicResource
authors:
  item: Pour-Rahimi F
  item: Nemat-Gorgani M
journal: Int J Biochem
pages: 53-61
published year: 1987
volume: 19
references: http://www.ncbi.nlm.nih.gov/pubmed/3569640

Multiple interactions of lysine-128 of Escherichia coli glutamate dehydrogenase revealed by site-directed mutagenesis studies.
type: BibliographicResource
authors:
  item: McPherson MJ
  item: Baron AJ
  item: Jones KM
  item: Price GJ
  item: Wootton JC
journal: Protein Eng
pages: 147-52
published year: 1988
volume: 2
references: http://www.ncbi.nlm.nih.gov/pubmed/3149742

Enzymatic in situ analysis by 1H-NMR of the hydrogen transfer stereospecificity of NAD(P)+-dependent dehydrogenases.
type: BibliographicResource
authors:
  item: Nakajima N
  item: Nakamura K
  item: Esaki N
  item: Tanaka H
  item: Soda K
journal: J Biochem (Tokyo)
pages: 515-7
published year: 1989
volume: 106
references: http://www.ncbi.nlm.nih.gov/pubmed/2575093

Transduction of enzyme-ligand binding energy into catalytic driving force.
type: BibliographicResource
authors:
  item: Fisher HF
  item: Singh N
journal: FEBS Lett
pages: 1-5
published year: 1991
volume: 294
references: http://www.ncbi.nlm.nih.gov/pubmed/1743279

1ch6A01
type: Pdb
catalytic residue: LYS 126
references: 1ch6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ch6

1ch6B01
type: Pdb
catalytic residue: LYS 126
references: 1ch6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ch6

1ch6C01
type: Pdb
catalytic residue: LYS 126
references: 1ch6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ch6

1ch6D01
type: Pdb
catalytic residue: LYS 126
references: 1ch6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ch6

1ch6E01
type: Pdb
catalytic residue: LYS 126
references: 1ch6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ch6

1ch6F01
type: Pdb
catalytic residue: LYS 126
references: 1ch6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ch6

1hwxA02
type: Pdb
catalytic residue: LYS 126
references: 1hwx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwx

1hwxB02
type: Pdb
catalytic residue: LYS 126
references: 1hwx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwx

1hwxC02
type: Pdb
catalytic residue: LYS 126
references: 1hwx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwx

1hwxD02
type: Pdb
catalytic residue: LYS 126
references: 1hwx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwx

1hwxE02
type: Pdb
catalytic residue: LYS 126
references: 1hwx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwx

1hwxF02
type: Pdb
catalytic residue: LYS 126
references: 1hwx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwx

1hwyA02
type: Pdb
catalytic residue: LYS 126
references: 1hwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwy

1hwyB02
type: Pdb
catalytic residue: LYS 126
references: 1hwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwy

1hwyC02
type: Pdb
catalytic residue: LYS 126
references: 1hwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwy

1hwyD02
type: Pdb
catalytic residue: LYS 126
references: 1hwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwy

1hwyE02
type: Pdb
catalytic residue: LYS 126
references: 1hwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwy

1hwyF02
type: Pdb
catalytic residue: LYS 126
references: 1hwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwy

1hwzA02
type: Pdb
catalytic residue: LYS 126
references: 1hwz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwz

1hwzB02
type: Pdb
catalytic residue: LYS 126
references: 1hwz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwz

1hwzC02
type: Pdb
catalytic residue: LYS 126
references: 1hwz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwz

1hwzD02
type: Pdb
catalytic residue: LYS 126
references: 1hwz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwz

1hwzE02
type: Pdb
catalytic residue: LYS 126
references: 1hwz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwz

1hwzF02
type: Pdb
catalytic residue: LYS 126
references: 1hwz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwz

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

NAD+
type: KeggSubstrate
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00003
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggProduct
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00004
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADPH
type: KeggProduct
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00005
references: CHEBI:16474
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

NADP+
type: KeggSubstrate
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00006
references: CHEBI:18009
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NH3
type: KeggProduct
compound type: amine group
compound type: organic ion
references: KEGG:C00014
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

glutamic dehydrogenase
type: KeggEnzyme

glutamate dehydrogenase [NAD(P)+]
type: KeggEnzyme