Enzyme

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     2. Transferases
        2.6 Transferring nitrogenous groups
            2.6.1 Transaminases
ID:2.6.1.21
Description:D-amino-acid transaminase.
Alternative Name: D-aspartic aminotransferase.
D-aspartate transaminase.
D-aspartate aminotransferase.
D-amino acid transaminase.
D-amino acid aminotransferase.
D-alanine-D-glutamate transaminase.
D-alanine transaminase.
D-alanine aminotransferase.
Prosite: PDOC00618;
PDB:
PDBScop
4DAA 8025187; 8037566; 8025187; 8037566;
3LQS 8025187; 8037566; 8025187; 8037566;
3DAA 8025187; 8037566; 8025187; 8037566;
1DAA 8025187; 8037566; 8025187; 8037566;
5I60 8024171; 8036550; 8024171; 8036550;
 » show all

Cath: 3.20.10.10; 3.30.470.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.6.1.21
BRENDA Enzyme Link: BRENDA 2.6.1.21
KEGG Enzyme Link: KEGG2.6.1.21
BioCyc Enzyme Link: BioCyc 2.6.1.21
ExPASy Enzyme Link: ExPASy2.6.1.21
EC2PDB Enzyme Link: EC2PDB 2.6.1.21
ExplorEnz Enzyme Link: ExplorEnz 2.6.1.21
PRIAM enzyme-specific profiles Link: PRIAM 2.6.1.21
IntEnz Enzyme Link: IntEnz 2.6.1.21
MEDLINE Enzyme Link: MEDLINE 2.6.1.21
MSA:

2.6.1.21;

Phylogenetic Tree:

2.6.1.21;

Uniprot:
M-CSA:
RHEA:15869 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[CH;+0:6](-[*:7])-[NH2;+0:8]>>[*:5]-[C;H0;+0:6](-[*:7])=[O;H0;+0:4].[*:1]-[CH;+0:2](-[*:3])-[NH2;+0:8]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization of the genes encoding D-amino acid transaminase and glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus sphaericus ATCC 10208.Fotheringham IG, Bledig SA, Taylor PP1998 Aug9696787
Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase.Peisach D, Chipman DM, Van Ophem PW, Manning JM, Ringe D1998 Apr 79538014
Substrate inhibition of D-amino acid transaminase and protection by salts and by reduced nicotinamide adenine dinucleotide: isolation and initial characterization of a pyridoxo intermediate related to inactivation.van Ophem PW, Erickson SD, Martinez del Pozo A, Haller I, Chait BT, Yoshimura T, Soda K, Ringe D, Petsko G, Manning JM1998 Mar 39485439
Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity.Sugio S, Petsko GA, Manning JM, Soda K, Ringe D1995 Aug 17626635
Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination.Tanizawa K, Masu Y, Asano S, Tanaka H, Soda K1989 Feb 152914916
Cloning and functional characterization of Arabidopsis thaliana D-amino acid aminotransferase--D-aspartate behavior during germination.Funakoshi M, Sekine M, Katane M, Furuchi T, Yohda M, Yoshikawa T, Homma H2008 Mar18318836