Methylaspartate ammonia-lyase

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In enzymology, a methylaspartate ammonia-lyase (EC 4.3.1.2) is an enzyme that catalyzes the chemical reaction

L-threo-3-methylaspartate $\rightleftharpoons$ mesaconate + NH₃

Hence, this enzyme has one substrate, L-threo-3-methylaspartate, and two products, mesaconate and NH₃.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-threo-3-methylaspartate ammonia-lyase (mesaconate-forming). Other names in common use include beta-methylaspartase, 3-methylaspartase, and L-threo-3-methylaspartate ammonia-lyase. This enzyme participates in c5-branched dibasic acid metabolism and nitrogen metabolism. It employs one cofactor, cobamide.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1KCZ, 1KD0, 1KKO, and 1KKR.

[edit] References

IUBMB entry for 4.3.1.2
BRENDA references for 4.3.1.2 (Recommended.)
PubMed references for 4.3.1.2
PubMed Central references for 4.3.1.2
Google Scholar references for 4.3.1.2
BARKER HA, SMYTH RD, WAWSZKIEWICZ EJ, LEE MN, WILSON RM (1958). "Enzymic preparation and characterization of an alpha-L-beta-methylaspartic acid". Arch. Biochem. Biophys. 78: 468–76. doi:10.1016/0003-9861(58)90371-0. PMID 13618029.
Bright HJ and Ingraham LL (1960). "The preparation of crystalline beta-methylaspartase". Biochim. Biophys. Acta 44: 586–588. doi:10.1016/0006-3002(60)91612-7.