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A carrot gene homologous to the ABI3 gene of Arabidopsis was isolated from a carrot somatic embryo cDNA library and designated C-ABI3. The sequence of C-ABI3 was very similar to those of ABI3 of Arabidopsis and VP1 of maize in certain conserved regions. The expression of C-ABI3 was detected specifically in embryogenic cells, somatic embryos and developing(More)
The mechanism of stereospecific conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Pseudomonas sp. strain NS671 was studied. The results indicated that the hydantoinase catalyzed the hydrolysis reaction of both D- and L-5-(2-methylthioethyl)hydantoin, and that the hydrolysis of the L-enantiomer proceeded preferentially compared(More)
A DNA fragment containing the gene for a thermostable hydantoinase was cloned from a thermophile, Bacillus stearothermophilus NS1122A in Escherichia coli. Nucleotide sequencing showed that the DNA fragment contains one open reading frame, which is predicted to encode a peptide of 471 amino acids, with a calculated molecular weight of 51,724. When the(More)
Pseudomonas sp. strain NS671, which produces L-amino acids asymmetrically from the corresponding racemic 5-substituted hydantoins, harbored a plasmid of 172 kb. Curing experiments suggest that this plasmid, designated pHN671, is responsible for the conversion of 5-substituted hydantoins to their corresponding L-amino acids by strain NS671. DNA fragments(More)
The hydantoin racemase gene of Pseudomonas sp. strain NS671 had been cloned and expressed in Escherichia coli. Hydantoin racemase was purified from the cell extract of the E. coli strain by phenyl-Sepharose, DEAE-Sephacel, and Sephadex G-200 chromatographies. The purified enzyme had an apparent molecular mass of 32 kDa as determined by sodium dodecyl(More)
DNA fragments containing the genes involved in the conversion of 5-substituted hydantoins to their corresponding L-amino acids have been cloned from the 172-kb native plasmid (pHN671) of Pseudomonas sp. strain NS671. The largest recombinant plasmid, designated pHPB14, encoded the ability to convert D-5-substituted hydantoins to the corresponding L-amino(More)
An N-carbamyl-L-amino acid amidohydrolase was purified from cells of Escherichia coli in which the gene for N-carbamyl-L-amino acid amidohydrolase of Pseudomonas sp. strain NS671 was expressed. The purified enzyme was homogeneous by the criterion of SDS-polyacrylamide gel electrophoresis. The results of gel filtration chromatography and SDS-polyacrylamide(More)
Phosphoglycerate mutase of Bacillus subtilis was purified to apparent homogeneity. It specifically required manganese ions for stability and activity, but it does not need 2,3-diphosphoglycerate as cofactor; the Km for Mn2+ is about 4.5 micrometer. Enzyme activity was inhibited by heavy-metal ions, 2,3-butanedione, and sulfhydryl agents. The mutase has a(More)
Thirty-two polymorphic microsatellite loci were indentified and characterized from the mysid Crustacea Mesopodopsis tenuipes Hanamura et al., 2008. The number of observed alleles per locus in 32 individuals collected from its type locality in Malaysia ranged from 2 to 22. The observed heterozygosity ranged from 0.031 to 0.906, while the expected(More)
Twenty-four microsatellite loci were isolated and characterized from the genome of Rasbora borapetensis. Flanking polymerase chain reaction primers were designed and used to amplify these loci in 32 individuals. All loci were polymorphic with allele numbers ranging from 2 to 27, observed heterozygosity from 0.031 to 1.000 and expected heterozygosity from(More)