Methylaspartate ammonia-lyase

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methylaspartate ammonia-lyase
1kko.png
X-ray structure of methylaspartate ammonia lyase. PDB entry 1kko [1]
Identifiers
EC no. 4.3.1.2
CAS no. 9033-26-5
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ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
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The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the chemical reaction

L-threo-3-methylaspartate mesaconate + 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 β-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.

Structural studies

Several structures of this enzyme have been deposited in the Protein Data Bank (linked in the infobox) which show it possesses a TIM barrel domain.

Related Research Articles

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<span class="mw-page-title-main">Transsulfuration pathway</span>

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In enzymology, a methylaspartate mutase is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">Isocitrate lyase</span>

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<span class="mw-page-title-main">Cys/Met metabolism PLP-dependent enzyme family</span>

In molecular biology, the Cys/Met metabolism PLP-dependent enzyme family is a family of proteins including enzymes involved in cysteine and methionine metabolism which use PLP (pyridoxal-5'-phosphate) as a cofactor.

References

  1. Levy, C. W.; Buckley, P. A.; Sedelnikova, S.; Kato, Y.; Asano, Y.; Rice, D. W.; Baker, P. J. (2002). "Insights into Enzyme Evolution Revealed by the Structure of Methylaspartate Ammonia Lyase". Structure. 10 (1): 105–13. doi: 10.1016/S0969-2126(01)00696-7 . PMID   11796115.