Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.4 Acting on the CH-NH2 group of donors
            1.4.1 With NAD+ or NADP+ as acceptor
ID:1.4.1.3
Description:Glutamate dehydrogenase (NAD(P)(+)).
Alternative Name: Glutamic dehydrogenase.
Prosite: PDOC00071;
PDB:
PDBScop
Cath: 1.10.287.140; 3.40.50.720; 3.40.50.10860;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.4.1.3
BRENDA Enzyme Link: BRENDA 1.4.1.3
KEGG Enzyme Link: KEGG1.4.1.3
BioCyc Enzyme Link: BioCyc 1.4.1.3
ExPASy Enzyme Link: ExPASy1.4.1.3
EC2PDB Enzyme Link: EC2PDB 1.4.1.3
ExplorEnz Enzyme Link: ExplorEnz 1.4.1.3
PRIAM enzyme-specific profiles Link: PRIAM 1.4.1.3
IntEnz Enzyme Link: IntEnz 1.4.1.3
MEDLINE Enzyme Link: MEDLINE 1.4.1.3
MSA:

1.4.1.3;

Phylogenetic Tree:

1.4.1.3;

Uniprot:
M-CSA:
RHEA:15133 H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:13].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[NH3;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
The catalytic role of aspartate in the active site of glutamate dehydrogenase.Dean JL, Wang XG, Teller JK, Waugh ML, Britton KL, Baker PJ, Stillman TJ, Martin SR, Rice DW, Engel PC1994 Jul 18037659
Biochemical characterization of two glutamate dehydrogenases with different cofactor specificities from a hyperthermophilic archaeon Pyrobaculum calidifontis.Wakamatsu T, Higashi C, Ohmori T, Doi K, Ohshima T2013 May23508687
Functional dissection of a trigger enzyme: mutations of the bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties.Gunka K, Newman JA, Commichau FM, Herzberg C, Rodrigues C, Hewitt L, Lewis RJ, Stülke J2010 Jul 2320630473
Probing the determinants of coenzyme specificity in Peptostreptococcus asaccharolyticus glutamate dehydrogenase by site-directed mutagenesis.Carrigan JB, Engel PC2007 Oct17850332
Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis.Khan MI, Ito K, Kim H, Ashida H, Ishikawa T, Shibata H, Sawa Y2005 Oct16244435
Properties of the thermostable glutamate dehydrogenase of the mesophilic anaerobe Peptostreptoccus asaccharolyticus purified by a novel method after over-expression in an Escherichia coli host.Carrigan JB, Coughlan S, Engel PC2005 Mar 115727821
Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase.Kim DW, Eum WS, Jang SH, Yoon CS, Kim YH, Choi SH, Choi HS, Kim SY, Kwon HY, Kang JH, Kwon OS, Cho SW, Park J, Choi SY2003 Nov 3014659072
The gdhB gene of Pseudomonas aeruginosa encodes an arginine-inducible NAD(+)-dependent glutamate dehydrogenase which is subject to allosteric regulation.Lu CD, Abdelal AT2001 Jan11133942

RHEA:11612 H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:13].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[NH3;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route.Tempest DW, Meers JL, Brown CM1970 Apr5420057
Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein.Miller RE, Stadtman ER1972 Nov 254565085
Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase.Ravasio S, Curti B, Vanoni MA2001 May 811331018
Glutamate synthase: a complex iron-sulfur flavoprotein.Vanoni MA, Curti B1999 Apr10357231