Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme, and sequence determination of the pyridoxal 5'-phosphate binding peptide.
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TL;DR: A wide occurrence of alpha,beta-diaminopropionate ammonia-lyase in bacteria and actinomycetes is found and no homology was found in either the amino acid sequence of the pyridoxal-P binding peptide or the amino-terminal amino acids sequence between the enzyme and other pyridine-P-dependent enzymes.
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About: This article is published in Journal of Biological Chemistry. The article was published on 15 Jan 1988. and is currently open access. The article focuses on the topics: Lysyl endopeptidase & Peptide sequence.
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Citations
Synthetic and Therapeutic Applications of Ammonia-lyases and Aminomutases
TL;DR: The discovery and mechanistic investigations of these commercially relevant enzymes are detailed, along with comparisons of their various applications as stand-alone catalysts, components of artificial biosynthetic pathways and biocatalytic or chemoenzymatic cascades, and therapeutic tools for the potential treatment of various pathologies.
Generation and biological characterization of membrane-bound, uncleavable murine tumor necrosis factor.
TL;DR: In this paper, mutational analysis of potential cleavage sites in murine TNF was carried out to compare the biological activity of membrane-bound versus soluble TNF, and the results indicated that membrane-based TNF cannot be passed from the 75kDa to the 55-kDa TNF receptor.
141
Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination.
TL;DR: D-Amino acid aminotransferase was found in several thermophilic Bacillus species and purified to homogeneity from the best producer, Bacillus sp.
93
Glucosamine-6-phosphate synthase from Escherichia coli: determination of the mechanism of inactivation by N3-fumaroyl-L-2,3-diaminopropionic derivatives.
TL;DR: A mechanistic investigation of the inactivation of Escherichia coli glucosamine-6-phosphate synthase by N3-(4-methoxyfumaroyl)-L-2,3-diaminopropionate (FMDP) was undertaken, and a pathway that is in perfect agreement with the biochemical results was proposed.
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From microbiology to cancer biology: the Rid protein family prevents cellular damage caused by endogenously generated reactive nitrogen species.
Diana M. Downs,Dustin C. Ernst +1 more
TL;DR: The data show that 2‐aminoacrylate (2AA), a reactive enamine intermediate generated by some pyridoxal 5′‐phosphate‐dependent enzymes, accumulates in the absence of RidA and the effect of this biochemical activity on the metabolic network, which impacts organism fitness.
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