EC Tree |
1. Oxidoreductases |
1.8 Acting on a sulfur group of donors |
1.8.3 With oxygen as acceptor |
ID: | 1.8.3.5 |
---|---|
Description: | Prenylcysteine oxidase. |
Alternative Name: |
Prenylcysteine lyase. |
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 1.8.3.5 |
BRENDA Enzyme Link: | BRENDA 1.8.3.5 |
KEGG Enzyme Link: | KEGG1.8.3.5 |
BioCyc Enzyme Link: | BioCyc 1.8.3.5 |
ExPASy Enzyme Link: | ExPASy1.8.3.5 |
EC2PDB Enzyme Link: | EC2PDB 1.8.3.5 |
ExplorEnz Enzyme Link: | ExplorEnz 1.8.3.5 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.8.3.5 |
IntEnz Enzyme Link: | IntEnz 1.8.3.5 |
MEDLINE Enzyme Link: | MEDLINE 1.8.3.5 |
RHEA:53892 | an S-prenyl-L-cysteine + H2O + O2 = a prenal + H2O2 + L-cysteine |
RULE(radius=1) | [*:1]-[S;H0;+0:2]-[CH2;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:4]-[CH;+0:3]=[O;H0;+0:7].[*:1]-[SH;+0:2].[OH;+0:5]-[OH;+0:6] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Isolation and characterization of a prenylcysteine lyase from bovine brain. | Zhang L, Tschantz WR, Casey PJ | 1997 Sep 12 | 9287348 |
Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase. | Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ | 2001 Jan 26 | 11078725 |
RHEA:14361 | H2O + O2 + S-prenyl-L-cysteine = 3-methyl-2-butenal + H2O2 + L-cysteine |
RULE(radius=1) | [*:1]-[S;H0;+0:2]-[CH2;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:4]-[CH;+0:3]=[O;H0;+0:7].[*:1]-[SH;+0:2].[OH;+0:5]-[OH;+0:6] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Isolation and characterization of a prenylcysteine lyase from bovine brain. | Zhang L, Tschantz WR, Casey PJ | 1997 Sep 12 | 9287348 |
Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase. | Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ | 2001 Jan 26 | 11078725 |