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Purification, Characterization and Inhibition of Alanine Racemase from a Pathogenic Strain of Streptococcus iniae
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Purification, Characterization and Inhibition of Alanine Racemase from a Pathogenic Strain of Streptococcus iniae
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Journal Article
Purification, Characterization and Inhibition of Alanine Racemase from a Pathogenic Strain of Streptococcus iniae
2019
Overview
is a pathogenic and zoonotic bacteria that impacted high mortality to many fish species as well as capable of causing serious disease to humans. Alanine racemase (Alr, EC 5.1.1.1) is a pyridoxal-5’-phosphate (PLP)-containing homodimeric enzyme that catalyzes the racemization of L-alanine and D-alanine. In this study, we purified alanine racemase from
that was isolated from an infected Chinese sturgeon (
), as well as determined its biochemical characteristics and inhibitors. The
gene has an open reading frame (ORF) of 1107 bp, encoding a protein of 369 amino acids, which has a molecular mass of 40 kDa. The enzyme has optimal activity at a temperature of 35°C and a pH of 9.5. It belongs to the PLP-dependent enzymes family and is highly specific to L-alanine.
Alr (SiAlr) could be inhibited by some metal ions, hydroxylamine and dithiothreitol (DTT). The kinetic parameters
and
of the enzyme were 33.11 mM, 2426 units/mg for L-alanine, and 14.36 mM, 963.6 units/mg for D-alanine. Finally, the 50% inhibitory concentrations (IC
) values and antibiotic activity of two alanine racemase inhibitors (homogentisic acid and hydroquinone), were determined and found to be effective against both Gram-positive and Gram-negative bacteria employed in this study.
Publisher
Sciendo,Exeley Inc,De Gruyter Brill Sp. z o.o., Paradigm Publishing Services
Subject
/ Alanine
/ Alanine Racemase - antagonists & inhibitors
/ Alanine Racemase - chemistry
/ Alanine Racemase - isolation & purification
/ Alanine Racemase - metabolism
/ ALR gene
/ Bacteria
/ Bacterial Proteins - antagonists & inhibitors
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Cloning
/ E coli
/ Enzyme Inhibitors - chemistry
/ Enzymes
/ Humans
/ hydroquinone and peptidoglycan
/ Kinetics
/ Plasmids
/ Proteins
/ Streptococcal Infections - microbiology
/ Streptococcus iniae - chemistry
/ Streptococcus iniae - enzymology
/ Sturgeon
/ Vaccines
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