Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Herbert Hottinger"'
Autor:
Sunil Kochhar, Victor S. Lamzin, Adelia Razeto, JacquesâEdouard Germond, Herbert Hottinger, Michèle Delley
Publikováno v:
European Journal of Biochemistry. 267:1633-1639
The role of three histidine residues (His205, His296 and His303) and Asp259, important for the catalysis of NAD+-specific D-lactate dehydrogenase, was investigated using site-directed mutagenesis. None of these residues is presumed to be involved in
Autor:
Tony Atkinson, Paul G. Taylor, Nathalie Chuard, Herbert Hottinger, Michael D. Scawen, David J. Nicholls, Sunil Kochhar
Publikováno v:
European Journal of Biochemistry. 208:799-805
NAD(+)-dependent D-lactate dehydrogenase from Lactobacillus helveticus was purified to apparent homogeneity, and the sequence of the first 36 amino acid residues determined. Using forward and reverse oligonucleotide primers, based on the N-terminal s
Publikováno v:
Biochemical and Biophysical Research Communications. 184:60-66
A comparison of the primary structures of NAD(+)-dependent D-lactate dehydrogenase with L-lactate dehydrogenase and L-malate dehydrogenase failed to show any sequence similarity. However, D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei,
Publikováno v:
Journal of Biological Chemistry. 267:8499-8513
The NAD(+)-dependent D-lactate dehydrogenase was purified to apparent homogeneity from Lactobacillus bulgaricus and its complete amino acid sequence determined. Two gaps in the polypeptide chain (10 residues) were filled by the deduced amino acid seq
Autor:
Adelia Razeto, Keith S. Wilson, Herbert Hottinger, Miroslava Dauter, Sunil Kochhar, Victor S. Lamzin
Publikováno v:
Journal of molecular biology. 318(1)
NAD-dependent Lactobacillus bulgaricus d -Lactate dehydrogenase ( d -LDHb) catalyses the reversible conversion of pyruvate into d -lactate. Crystals of d -LDHb complexed with NADH were grown and X-ray data collected to 2.2 A. The structure of d -LDHb
Publikováno v:
Biochimie. 76(1)
The nifS gene was first identified in nitrogen-fixing bacteria where its protein product is essential for efficient nitrogen fixation. Here, we demonstrate that a nifS-like gene also occurs in Lactobacillus bulgaricus, an organism which does not fix
Publikováno v:
The Journal of biological chemistry. 267(28)
Recently, we amplified the Lactobacillus bulgaricus NAD(+)-dependent D-lactate dehydrogenase gene by the polymerase chain reaction, cloned and overexpressed it in Escherichia coli (Kochhar, S., Chuard, N., and Hottinger, H. (1992) Biochem. Biophys. R
Publikováno v:
Biochemical and biophysical research communications. 185(2)
The Lactobacillus bulgaricus NAD(+)-dependent D-lactate dehydrogenase gene was amplified by the polymerase chain reaction and cloned into an Escherichia coli expression plasmid pKK223.3. Attempts to clone the full-length chromosomal DNA encoding D-la
Publikováno v:
Applied and environmental microbiology. 56(6)
From a genomic DNA library of Lactobacillus delbrueckii subsp. bulgaricus, a clone was isolated which complements a leucine auxotrophy of an Escherichia coli strain (GE891). Subsequent analysis of the clone indicated that it could serve as a specific
Publikováno v:
Genetics. 87:471-489
The genetic maps of the fission yeast Schizosaccharomyces pombe were extended through the use of haploidization (spontaneous or induced by m-fluorophenylalanine), as well as by tetrad, random spore and mitotic analysis. A new diploidization method ut