Crystal structure of D-serine dehydratase from Escherichia coli
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چکیده
منابع مشابه
D-Serine dehydratase from Escherichia coli. Essential arginine residue at the pyridoxal 5'-phosphate binding site.
D-Serine apodehydratase from Escherichia coli is rapidly inactivated by butanedione in K+ borate buffer or by phenylglyoxal in K+ phosphate buffer at pH 8, 25 degrees. Pyridoxal-P protects against the inactivation. Modification of the apoenzyme abolishes its ability to bind the cofactor, pyridoxal-P, but the apparent Km for the substrate, D-serine, is not altered. The concentration dependence o...
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D-serine is a physiological co-agonist of the N-methyl-D-aspartate receptor. It regulates excitatory neurotransmission, which is important for higher brain functions in vertebrates. In mammalian brains, D-amino acid oxidase degrades D-serine. However, we have found recently that in chicken brains the oxidase is not expressed and instead a D-serine dehydratase degrades D-serine. The primary stru...
متن کاملPurification and properties of D-serine dehydrase from Escherichia coli.
A procedure is described for obtaining crystalline o-serine dehydrase from a mutant of Escherichia coli which produces this enzyme constitutively. The enzyme appears pure by ultracentrifugal and electrophoretic criteria. In sucrose gradients, serine dehydrase sediments to the same position as horseradish peroxidase, indicating a molecular weight of about 40,000. This corresponds closely to its ...
متن کاملCrystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver.
L-serine dehydratase (SDH), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and L-threonine to yield pyruvate or 2-oxobutyrate. The crystal structure of L-serine dehydratase from human liver (hSDH) has been solved at 2.5 A-resolution by molecular replacement. The structure is a homodimer and reveals a fold typical for beta-family...
متن کاملA novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae.
YGL196W of Saccharomyces cerevisiae encodes a putative protein that is unidentified but is predicted to have a motif similar to that of the N-terminal domain of the bacterial alanine racemase. In the present study we found that YGL196W encodes a novel D-serine dehydratase, which belongs to a different protein family from that of the known bacterial enzyme. The yeast D-serine dehydratase purifie...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
سال: 2012
ISSN: 1570-9639
DOI: 10.1016/j.bbapap.2011.10.017