3-Methylaspartate Ammonia-lyase from a Facultative Anaerobe, Strain YG-1002

Overview

Journal Appl Microbiol Biotechnol

Specialties Biomedical Engineering
Biotechnology
Microbiology

Date 1995 Oct 1

PMID 7576557

Citations 3

Authors

Y Kato

Y Asano

Affiliations

Soon will be listed here.

Abstract

3-Methylaspartase was purified 24-fold and crystallized from the crude extract of the cells of a facultative anaerobic bacterium from soil, strain YG-1002. The molecular mass of the native enzyme was about 84 kDa and that of the subunit was about 42 kDa. The pH optimum for the deamination reaction of (2S, 3S)-3-methylaspartic acid and those for the amination reaction of mesaconic acid were 9.7 and 8.5; its optimum temperature was 50 degrees C. The enzyme was stable at pH 5.5-11.0 and up to 50 degrees C. The enzyme required both divalent and monovalent cations such as Mg2+ and K+. The enzyme was inhibited by sulfhydryl reagents, metal-chelating reagents and some divalent cations. The enzyme catalyzed the reversible amination/deamination reactions between several 3-substituted (S)-aspartic acids and their corresponding fumaric acid derivatives. The enzyme preferentially acted on (2S, 3S)-3-methylaspartic acid and mesaconic acid in the deamination and the amination reactions respectively. The enzyme showed high similarities in several enzymological properties and N-terminal amino acid sequence with 3-methylaspartase from an obligate anaerobic bacterium Clostridium tetanomorphum.

Citing Articles

Mesaconase/Fumarase FumD in Escherichia coli O157:H7 and Promiscuity of Escherichia coli Class I Fumarases FumA and FumB.

Kronen M, Berg I PLoS One. 2015; 10(12):e0145098.

PMID: 26658641 PMC: 4682846. DOI: 10.1371/journal.pone.0145098.

Characterization of a thermostable methylaspartate ammonia lyase from Carboxydothermus hydrogenoformans.

Raj H, Puthan Veetil V, Szymanski W, Dekker F, Quax W, Feringa B Appl Microbiol Biotechnol. 2011; 94(2):385-97.

PMID: 22005738 PMC: 3310078. DOI: 10.1007/s00253-011-3615-6.

Purification and characterization of beta-methylaspartase from Fusobacterium varium.

Bearne S, White R, MacDonnell J, Bahrami S, Gronlund J Mol Cell Biochem. 2001; 221(1-2):117-26.

PMID: 11506174 DOI: 10.1023/a:1010938111292.

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