T. Kamiryo

Publications49
h-index22
Citations1,230
Highly Influential Citations25
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Evidence that acyl coenzyme A synthetase activity is required for repression of yeast acetyl coenzyme A carboxylase by exogenous fatty acids.
TLDR
Results indicate that the activation of exogenous fatty acid is required for the repression of acetyl-CoA carboxylase, supporting the view that the repressive effect is mediated by some compound metabolically derived from fatty acid.
Mechanism of Action and Development of Resistance to a New Amidino Penicillin
TLDR
The mechanism of killing of Escherichia coli by a novel beta-lactam antibiotic, an amidino penicillin, has been investigated and mutants resistant to the amidino Penicillin were isolated and several were studied in detail.
Absence of DNA in peroxisomes of Candida tropicalis
TLDR
The purification procedure includes the effective conversion of cells to spheroplasts with Zymolyase and sodium sulfite and the separation of the organelles at extremely low ionic strength.
Acyl-coenzyme-A synthetase I from Candida lipolytica. Purification, properties and immunochemical studies.
TLDR
Studies with the use of specific antibody to acyl-CoA synthetase I have indicated that this enzyme is immunochemically distinguishable from acyl -CoA Synthetase II.
Two acyl-coenzyme A oxidases in peroxisomes of the yeast Candida tropicalis: primary structures deduced from genomic DNA sequence.
TLDR
Although the two polypeptides were significantly homologous throughout their sequences, the local homologies in two regions out of five were markedly diverged from the average; the homology in the second region was 93%, whereas that in the fourth one was only 24%.
Thiolase involved in bile acid formation.
TLDR
The production of cholic acid and chenodeoxycholic acid from the precursors on incubation with the bifunctional protein and sterol carrier protein x or P-44 was confirmed by gas chromatography.
Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate.
TLDR
The expression and localization of type-II 3-oxoacyl-CoA thiolase in the nematode Caenorhabditis elegans are examined, suggesting their common physiological roles.
Candida lipolytica mutants defective in an acyl-coenzyme A synthetase: isolation and fatty acid metabolism.
TLDR
Analysis of the fatty acid composition of the lipids from the mutant cells grown on odd-chain-length fatty acid as well as [14C]oleic acid incorporation studies have shown that the mutants cells, unlike the wild-type cells, cannot incorporate exogenous fatty acids as a whole into cellular lipids, but utilize the fatty acids that is synthesized de novo from acetyl-CoA produced by degradation of exogenous acids.
Separation and characterization of two long-chain acyl-CoA synthetases from Candida lipolytica.
TLDR
The results indicate that C. lipolytica cells grown on·oleic acid possess two distinct long-chain acyl-CoA synthetases, which supports the concept, based on the phenotype of the mutants mentioned above, that acy-Co a synthetase I is responsible for the production of acyl CoA to be utilized for the synthesis of cellular lipids.
[39] Long-chain acyl-CoA synthetases I and II from Candida lipolytica: EC 6.2.1.3 acid:CoA ligase (AMP-forming)
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