ID: | 2.1.1.142 |
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Description: | Cycloartenol 24-C-methyltransferase. |
Alternative Name: |
Sterol C-methyltransferase. |
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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 2.1.1.142 |
BRENDA Enzyme Link: | BRENDA 2.1.1.142 |
KEGG Enzyme Link: | KEGG2.1.1.142 |
BioCyc Enzyme Link: | BioCyc 2.1.1.142 |
ExPASy Enzyme Link: | ExPASy2.1.1.142 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.142 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.142 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.142 |
IntEnz Enzyme Link: | IntEnz 2.1.1.142 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.142 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:13137 | cycloartenol + S-adenosyl-L-methionine = (24R)-24-methylcycloart-25-en-3beta-ol + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[CH;+0:2]=[C;H0;+0:3](-[*:4])-[CH3;+0:5].[*:6]-[S+;H0:7](-[*:8])-[CH3;+0:9]>>[*:1]-[CH;+0:2](-[CH3;+0:9])-[C;H0;+0:3](-[*:4])=[CH2;+0:5].[*:6]-[S;H0;+0:7]-[*:8] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Sterol C-methyl transferase from Prototheca wickerhamii mechanism, sterol specificity and inhibition. | Mangla AT, Nes WD | 2000 May | 10882005 |