“Methylmalonyl-CoA decarboxylase”的意思、由来-开放百科全书

词条

Methylmalonyl-CoA decarboxylase

释义

Structural studies
References

{{enzyme
| Name = methylmalonyl-CoA decarboxylase
| EC_number = 4.1.1.41
| CAS_number = 37289-44-4
| IUBMB_EC_number = 4/1/1/41
| GO_code = 0004492
| image = 1ef8.jpg
| width = 270
| caption = Methylmalonyl CoA decarboxylase trimer, E.Coli
}}

In enzymology, a methylmalonyl-CoA decarboxylase ({{EC number|4.1.1.41}}) is an enzyme that catalyzes the chemical reaction

(S)-methylmalonyl-CoA propanoyl-CoA + CO₂

Hence, this enzyme has one substrate, (S)-methylmalonyl-CoA, and two products, propanoyl-CoA and CO₂.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming). Other names in common use include propionyl-CoA carboxylase, propionyl coenzyme A carboxylase, methylmalonyl-coenzyme A decarboxylase, (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect], and (S)-methylmalonyl-CoA carboxy-lyase. This enzyme participates in propanoate metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1EF8}} and {{PDB link|1EF9}}.

References

{{cite journal | vauthors = Galivan JH, Allen SH | date = 1968 | title = Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus | journal = J. Biol. Chem. | volume = 243 | pages = 1253–61 | pmid = 5646172 | issue = 6 }}
{{cite journal | vauthors = Hilpert W, Dimroth P | date = 1982 | title = Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient | journal = Nature | volume = 296 | pages = 584–5 | pmid = 7070502 | doi = 10.1038/296584a0 | issue = 5857 }}
{{cite journal | vauthors = Hoffmann A, Hilpert W, Dimroth P | date = 1989 | title = The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens | journal = Eur. J. Biochem. | volume = 179 | pages = 645–50 | pmid = 2920730 | doi = 10.1111/j.1432-1033.1989.tb14596.x | issue = 3 }}

2 : EC 4.1.1|Enzymes of known structure

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