EC Tree |
4. Lyases |
4.5 Carbon-halide lyases |
4.5.1 Carbon-halide lyases (only sub-subclass identified to date) |
ID: | 4.5.1.2 |
---|---|
Description: | 3-chloro-D-alanine dehydrochlorinase. |
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.UniProtKB Enzyme Link: | UniProtKB 4.5.1.2 |
BRENDA Enzyme Link: | BRENDA 4.5.1.2 |
KEGG Enzyme Link: | KEGG4.5.1.2 |
BioCyc Enzyme Link: | BioCyc 4.5.1.2 |
ExPASy Enzyme Link: | ExPASy4.5.1.2 |
EC2PDB Enzyme Link: | EC2PDB 4.5.1.2 |
ExplorEnz Enzyme Link: | ExplorEnz 4.5.1.2 |
PRIAM enzyme-specific profiles Link: | PRIAM 4.5.1.2 |
IntEnz Enzyme Link: | IntEnz 4.5.1.2 |
MEDLINE Enzyme Link: | MEDLINE 4.5.1.2 |
RHEA:18873 | 3-chloro-D-alanine + H2O = chloride + H(+) + NH4(+) + pyruvate |
RULE(radius=1) | [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[Cl;H0;+0:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](-[CH3;+0:4])=[O;H0;+0:6].[Cl-;H0:5].[NH3;+0:3] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Synthesis of D-cysteine from 3-chloro-D-alanine and hydrogen sulfide by 3-chloro-D-alanine hydrogen chloride-lyase (deaminating) of Pseudomonas putida. | Yamada H, Nagasawa T, Ohkishi H, Kawakami B, Tani Y | 1981 Jun 16 | 6791643 |
Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. | Nagasawa T, Ishii T, Yamada H | 1988 | 3132906 |