Enzyme

Download
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.

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 1.8.3.5
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
MSA:

1.8.3.5;

Phylogenetic Tree:

1.8.3.5;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed ID
Isolation and characterization of a prenylcysteine lyase from bovine brain.Zhang L, Tschantz WR, Casey PJ1997 Sep 129287348
Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ2001 Jan 2611078725

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

References

TitleAuthorsDatePubMed ID
Isolation and characterization of a prenylcysteine lyase from bovine brain.Zhang L, Tschantz WR, Casey PJ1997 Sep 129287348
Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ2001 Jan 2611078725