“Methenyltetrahydrofolate cyclohydrolase”的意思、由来-开放百科全书

词条

Methenyltetrahydrofolate cyclohydrolase

释义

Synonyms
Structural studies
References

{{enzyme
| Name = methenyltetrahydrofolate cyclohydrolase
| EC_number = 3.5.4.9
| CAS_number = 9027-97-8
| IUBMB_EC_number = 3/5/4/9
| GO_code = 0004477
| image = 1dib.jpg
| width = 270
| caption = Methenyltetrahydrofolate cyclohydrolase dimer, Human
}}

In enzymology, a methenyltetrahydrofolate cyclohydrolase ({{EC number|3.5.4.9}}) is an enzyme that catalyzes the chemical reaction

5,10-methenyltetrahydrofolate + H₂O 10-formyltetrahydrofolate

Thus, the two substrates of this enzyme are 5,10-methenyltetrahydrofolate and H₂O, whereas its product is 10-formyltetrahydrofolate.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines.

This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.

Synonyms

The systematic name of this enzyme class is 5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing).

Other names in common use include:

Citrovorum factor cyclodehydrase
cyclohydrolase
formyl-methenyl-methylenetetrahydrofolate synthetase (combined).

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1A4I}}, {{PDB link|1DIA}}, {{PDB link|1DIB}}, {{PDB link|1DIG}}, {{PDB link|2C2X}}, and {{PDB link|2C2Y}}.

References

{{cite journal | vauthors = Rabinowitz JC, Pricer WE | date = 1956 | title = The enzymatic synthesis of N10-formyltetrahydrofolic acid and its role in ATP formation during formiminoglycine degradation | journal = J. Am. Chem. Soc. | volume = 78 | pages = 4176–4178 | doi = 10.1021/ja01597a094 | issue = 16 }}
{{cite journal | vauthors = Tabor H, Wyngarden L | title = The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid | journal = The Journal of Biological Chemistry | volume = 234 | issue = 7 | pages = 1830–46 | date = July 1959 | pmid = 13672973 }}

{{Carbon-nitrogen non-peptide hydrolases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{3.5-enzyme-stub}}

2 : EC 3.5.4|Enzymes of known structure

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