| Structural highlights
Function
ASPA_BACSP Catalyzes the reversible conversion of L-aspartate to fumarate and ammonia (PubMed:10334861, PubMed:10712618, PubMed:18844200, PubMed:19490103). Is highly specific for L-aspartate in the deamination reaction, and cannot use alternative substrates such as D-aspartic acid, alpha-methyl-DL-aspartic acid, beta-methyl-DL-aspartic acid or L-glutamate (PubMed:18844200). In the reverse reaction, alternative nucleophiles (such as hydroxylamine, hydrazine, methoxylamine and methylamine) can replace ammonia in vitro, leading to the formation of N-substituted aspartic acid derivatives (PubMed:18844200).[1] [2] [3] [4]
References
- ↑ Kawata Y, Tamura K, Yano S, Mizobata T, Nagai J, Esaki N, Soda K, Tokushige M, Yumoto N. Purification and characterization of thermostable aspartase from Bacillus sp. YM55-1. Arch Biochem Biophys. 1999 Jun 1;366(1):40-6. PMID:10334861 doi:10.1006/abbi.1999.1186
- ↑ Kawata Y, Tamura K, Kawamura M, Ikei K, Mizobata T, Nagai J, Fujita M, Yano S, Tokushige M, Yumoto N. Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue. Eur J Biochem. 2000 Mar;267(6):1847-57. PMID:10712618 doi:10.1046/j.1432-1327.2000.01190.x
- ↑ Weiner B, Poelarends GJ, Janssen DB, Feringa BL. Biocatalytic enantioselective synthesis of N-substituted aspartic acids by aspartate ammonia lyase. Chemistry. 2008;14(32):10094-100. PMID:18844200 doi:10.1002/chem.200801407
- ↑ Puthan Veetil V, Raj H, Quax WJ, Janssen DB, Poelarends GJ. Site-directed mutagenesis, kinetic and inhibition studies of aspartate ammonia lyase from Bacillus sp. YM55-1. FEBS J. 2009 Jun;276(11):2994-3007. PMID:19490103 doi:10.1111/j.1742-4658.2009.07015.x
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