“Methylaspartate mutase”的意思、由来-开放百科全书

词条

Methylaspartate mutase

释义

Structural studies
References

{{enzyme
| Name = methylaspartate mutase
| EC_number = 5.4.99.1
| CAS_number = 9032-97-7
| IUBMB_EC_number = 5/4/99/1
| GO_code = 0050097
| image =
| width =
| caption =
}}

In enzymology, a methylaspartate mutase ({{EC number|5.4.99.1}}) is an enzyme that catalyzes the chemical reaction

L-threo-3-methylaspartate L-glutamate

Hence, this enzyme has one substrate, L-threo-3-methylaspartate, and one product, L-glutamate.

This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is L-threo-3-methylaspartate carboxy-aminomethylmutase. Other names in common use include glutamate mutase, glutamic mutase, glutamic isomerase, glutamic acid mutase, glutamic acid isomerase, methylaspartic acid mutase, beta-methylaspartate-glutamate mutase, and glutamate isomerase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, cobamide.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1B1A}}, {{PDB link|1BE1}}, {{PDB link|1CB7}}, {{PDB link|1CCW}}, {{PDB link|1FMF}}, {{PDB link|1I9C}}, {{PDB link|1ID8}}, and {{PDB link|2PWH}}.

References

{{cite journal | vauthors = BARKER HA, ROOZE V, SUZUKI F, IODICE AA | year = 1964 | title = THE GLUTAMATE MUTASE SYSTEM. ASSAYS AND PROPERTIES | journal = J. Biol. Chem. | volume = 239 | pages = 3260–6 | pmid = 14245371 }}
{{cite journal | vauthors = Weissbach H, Toohey J, Barker HA | year = 1959 | title = Isolation and properties of B12 coenzymes containing benzimidazole or dimethylbenzimidazole | journal = Proc. Natl. Acad. Sci. USA | volume = 45 | pages = 521–528 | doi = 10.1073/pnas.45.4.521 | issue = 4 | pmc = 222591 }}

3 : EC 5.4.99|Cobamide enzymes|Enzymes of known structure

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