T00011
type: Enzyme
cath: Helix Hairpins
cath: Leucine Dehydrogenase; Chain A, domain 1
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.4.1.3
uniprot: P00366
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 substrate: L-Glutamate
kegg substrate: H2O
kegg substrate: NAD+
kegg substrate: NADP+
kegg product: 2-Oxoglutarate
kegg product: NH3
kegg product: H+
kegg product: NADH
kegg product: NADPH
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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00011#12
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9772187
journal: Biochemistry
volume: 37
pages: 14585-90
published year: 1998
authors:
  item: Maniscalco SJ
  item: Saha SK
  item: Fisher HF
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.

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

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

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

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

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

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

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

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00011#20
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12324473
journal: J Biol Chem
volume: 277
pages: 46552-8
published year: 2002
authors:
  item: Zaganas I
  item: Spanaki C
  item: Karpusas M
  item: Plaitakis A
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.

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00011#21
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11950837
journal: J Biol Chem
volume: 277
pages: 26422-8
published year: 2002
authors:
  item: Zaganas I
  item: Plaitakis A
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.

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

glutamic dehydrogenase
type: KeggEnzyme

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