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排序方式: 共有341条查询结果,搜索用时 15 毫秒
1.
2.
K Watanabe Y Fujii H Ohkubo S Kuramitsu H Kagamiyama S Nakanishi O Hayaishi 《Biochemical and biophysical research communications》1991,181(1):272-278
The full-length bovine lung prostaglandin(PG) F synthase cDNA was constructed from partial cDNA clones and ligated into bacterial expression vector pUC8 to develop expression plasmid pUCPF1. This plasmid permitted the synthesis of bovine lung PGF synthase in Escherichia coli. The recombinant bacteria overproduced a 36-KDa protein that was recognized by anti-PGF synthase antibody, and the expressed protein was purified to apparent homogeneity. The expressed protein reduced not only carbonyl compounds including PGD2 and phenanthrenequinone but also PGH2; and the Km values for phenanthrenequinone, PGD2, and PGH2 of the expressed protein were 0.1, 100, and 8 microM, respectively, which are the same as those of the bovine lung PGF synthase. The protein produced PGF2 alpha from PGH2, and 9 alpha, 11 beta-PGF2 from PGD2 at different active sites. Moreover, the structure of the purified protein from Escherichia coli was essentially identical to that of the native enzyme in terms of C-terminal sequence, sulfhydryl groups, and CD spectra except that the nine amino acids provided by the lac Z' gene of the vector were fused to the N-terminus. These results indicate that the expressed protein is essentially identical to bovine lung PGF synthase. We confirmed that PGF synthase is a dual function enzyme catalyzing the reduction of PGH2 and PGD2 on a single enzyme and that it has one binding site for NADPH. 相似文献
3.
Carboxyl-terminal deletion analysis of the Streptococcus mutans glucosyltransferase-I enzyme 总被引:9,自引:0,他引:9
Sequential deletion of the carboxyl-terminal amino acids (including the six direct repeating units) of the glucosyltransferase-I (GTF-I) enzyme of Streptococcus mutans revealed differential effects on sucrase and GTF activities. Removal of all but one repeating unit resulted in a truncated enzyme with significant sucrase activity but no detectable GTF activity. These results are compatible with the presence of two functional domains in the enzyme. 相似文献
4.
The streptococcal transposon Tn917 was demonstrated to transpose in Escherichia coli from the Bacillus subtilis-E. coli shuttle plasmid pHK1207 into an F' plasmid derivative. Subsequently, a second round of transposition from the F' plasmid into pACYC184 could be readily demonstrated. These results represent the initial demonstration of the transposition of a gram-positive transposon in a gram-negative bacterium at a relatively high frequency. 相似文献
5.
Cytosolic and mitochondrial isozymes of aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase [EC 2.6.1.1] ) were purified to homogeneity from rabbit liver. The rabbit liver isozymes were closely similar to the corresponding isozymes from other sources, including human heart, pig heart, chicken heart, and rat liver, in their molecular weights, absorption spectra, amino acid compositions, isoelectric points, and Michaelis constants for the substrates. The NH2-terminal amino acid sequences of rabbit liver isozymes were identified up to 30 residues, and showed some differences from those of the corresponding isozymes obtained from other animals so far studied. 相似文献
6.
Genetic exchange between oral streptococci during mixed growth 总被引:6,自引:0,他引:6
To determine whether oral streptococci might exchange genetic information in the oral cavity, paired transformable strains of Streptococcus mutans, Streptococcus sanguis and Streptococcus milleri were growth together. Chromosomal and plasmid-borne antibiotic resistance markers could be readily transferred from S. mutans GS-5 to S. milleri NCTC 10707 or S. sanguis Challis during mixed growth. However, no exchange from the latter two organisms to strain GS-5 could be detected under these conditions. The transfer of genetic information from S. sanguis to S. milleri was also observed. 相似文献
7.
The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases 总被引:10,自引:0,他引:10
K Tanizawa S Asano Y Masu S Kuramitsu H Kagamiyama H Tanaka K Soda 《The Journal of biological chemistry》1989,264(5):2450-2454
The gene for thermostable D-amino acid aminotransferase from a thermophile, Bacillus species YM-1 was cloned and expressed efficiently in Escherichia coli. The entire covalent structure of the enzyme was determined from the nucleotide sequence of the cloned gene and mostly confirmed by amino acid sequences of tryptic peptides from the gene product. The polypeptide is composed of 282 amino acid residues with a calculated molecular weight of 32,226. Comparison of the primary structure with those of various proteins registered in a protein data bank revealed a significant sequence homology between D-amino acid aminotransferase and the L-branched chain amino acid aminotransferase of E. coli (Kuramitsu, S., Ogawa, T., Ogawa, H., and Kagamiyama, H. (1985) J. Biochem. (Tokyo) 97, 993-999); the active site lysyl residue is located in an equivalent position in both enzyme sequences of similar size. Despite the difference in subunit composition and no immunochemical cross-reactivity, the sequences of the two enzymes show similar hydropathy profiles, and spectrophotometric properties of the enzyme-bound cofactor are also similar. The sequence homology suggests that the structural genes for D-amino acid and L-branched chain amino acid aminotransferases evolved from a common ancestral gene. 相似文献
8.
9.
Characterization of a thermostable DNA photolyase from an extremely thermophilic bacterium, Thermus thermophilus HB27.
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The photolyase gene from Thermus thermophilus was cloned and sequenced. The characteristic absorption and fluorescence spectra of the purified T. thermophilus photolyase suggested that the protein has flavin adenine dinucleotide as a chromophore. The second chromophore binding site was not conserved in T. thermophilus photolyase. The purified enzyme showed light-dependent photoreactivation activity in vitro at 35 and 65 degrees C and was stable when subjected to heat and acidic pH. 相似文献
10.
Sequence analysis and characterization of the Porphyromonas gingivalis prtC gene, which expresses a novel collagenase activity. 总被引:14,自引:0,他引:14
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In order to examine the potential role of bacterial collagenases in periodontal tissue destruction, we recently isolated a gene, prtC, from Porphyromonas gingivalis ATCC 53977, which expressed collagenase activity (N. Takahashi, T. Kato, and H. K. Kuramitsu, FEMS Microbiol. Lett. 84:135-138, 1991). The nucleotide sequence of the gene has been determined, and the deduced amino acid sequence corresponds to a basic protein of 37.8 kDa. In addition, Southern blot analysis indicated that the prtC gene is conserved among the three major serotypes of P. gingivalis. The enzyme has been purified to near homogeneity from Escherichia coli clone NTS1 following Mono Q anion exchange and sequential gel filtration chromatography. The molecular mass of the purified enzyme was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be ca. 35 kDa, and the active enzyme behaved as a dimer following gel filtration chromatography. The collagenase degraded soluble and reconstituted fibrillar type I collagen, heat-denatured type I collagen, and azocoll but not gelatin or the synthetic collagenase substrate 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg. Enzyme activity was enhanced by Ca2+ and inhibited by EDTA, sulfhydryl-blocking agents, and the salivary peptide histatin. Preliminary evidence for the existence of a second collagenase expressed by strain 53977 was also obtained. 相似文献