methenyltetrahydromethanopterin cyclohydrolase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Methenyltetrahydromethanopterin cyclohydrolase trimer, Archaeoglobus fulgidus | |||||||||
Identifiers | |||||||||
EC no. | 3.5.4.27 | ||||||||
CAS no. | 99533-50-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
In enzymology, a methenyltetrahydromethanopterin cyclohydrolase (EC 3.5.4.27) is an enzyme that catalyzes the chemical reaction
- 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O 5-formyl-5,6,7,8-tetrahydromethanopterin
Thus, the two substrates of this enzyme are 5,10-methenyl-5,6,7,8-tetrahydromethanopterin and H2O, whereas its product is 5-formyl-5,6,7,8-tetrahydromethanopterin.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 5,10-methenyltetrahydromethanopterin 10-hydrolase (decyclizing). Other names in common use include 5,10-methenyltetrahydromethanopterin cyclohydrolase, N5,N10-methenyltetrahydromethanopterin cyclohydrolase, and methenyl-H4MPT cyclohydrolase. This enzyme participates in folate biosynthesis.
References
- Donnelly MI, Escalante-Semerena JC, Rinehart KL, Wolfe RS (1985). "Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of Methanobacterium". Arch. Biochem. Biophys. 242 (2): 430–9. doi:10.1016/0003-9861(85)90227-9. PMID 4062290.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
---|---|
3.5.1: Linear amides / Amidohydrolases | |
3.5.2: Cyclic amides/ Amidohydrolases | |
3.5.3: Linear amidines/ Ureohydrolases | |
3.5.4: Cyclic amidines/ Aminohydrolases | |
3.5.5: Nitriles/ Aminohydrolases | |
3.5.99: Other |
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This EC 3.5 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |