IPR006395
Methylaspartate ammonia-lyase
InterPro entry
Short name | Me_Asp_am_lyase |
Overlapping homologous superfamilies |
Description
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. This reaction is part of the main catabolic pathway for glutamate. MAL belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion
[2, 3, 1].
References
1.3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae. Kato Y, Asano Y. Arch. Microbiol. 168, 457-63, (1997). View articlePMID: 9385136
2.The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH. J. Biol. Chem. 277, 8306-11, (2002). View articlePMID: 11748244
3.Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase. Levy CW, Buckley PA, Sedelnikova S, Kato Y, Asano Y, Rice DW, Baker PJ. Structure 10, 105-13, (2002). View articlePMID: 11796115
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entries
- SFLD:SFLDF00007
- CDD:cd03314
- PIRSF:PIRSF017107
- NCBIfam:TIGR01502
Representative structure
1kko: CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE