Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue.
- M. Kobayashi, N. Yanaka, T. Nagasawa, H. Yamada
- Biology, ChemistryBiochemistry
- 22 September 1992
Peptides obtained by cleavage of a Rhodococcus rhodochrous K22 nitrilase, which acts on aliphatic nitriles such as acrylonitrile, crotonitrile), have been sequenced and it is shown that this cysteinyl residue is essential for the catalytic activity.
Purification and characterization of a novel nitrilase of Rhodococcus rhodochrous K22 that acts on aliphatic nitriles
- M. Kobayashi, N. Yanaka, T. Nagasawa, H. Yamada
- Chemistry, BiologyJournal of Bacteriology
- 1 September 1990
A novel nitrilase that preferentially catalyzes the hydrolysis of aliphatic nitriles to the corresponding carboxylic acids and ammonia was found in the cells of a facultative crotononitrile-utilizing actinomycete isolated from soil, identified as Rhodococcus rhodochrous K22.
High protein buckwheat flour suppresses hypercholesterolemia in rats and gallstone formation in mice by hypercholesterolemic diet and body fat in rats because of its low protein digestibility.
- H. Tomotake, N. Yamamoto, N. Kato
- Biology, MedicineNutrition (Burbank, Los Angeles County, Calif.)
- 1 February 2006
Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue.
- M. Kobayashi, H. Komeda, N. Yanaka, T. Nagasawa, H. Yamada
- Biology, ChemistryJournal of Biological Chemistry
- 15 October 1992
Mammalian Glycerophosphodiester Phosphodiesterases
- N. Yanaka
- BiologyBioscience, biotechnology and biochemistry
- 23 August 2007
It is found that expression of GDE3 is significantly up-regulated during osteoblast differentiation and is involved in morphological changes of cells, indicating that the GP-PDE superfamily in mammals might be a pharmacological target in the future.
Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene.
Comparison of genomic organization with the rod photoreceptor phosphodiesterase beta-subunit gene (PDE6B), which is another kind of cGMP-specific phosphodiestersterase, has shown that the PDE5A and PDE6B genes are very similar in their relative exon intron organization.
Identification and physiological evaluation of the components from citrus fruits as potential drugs for anti-corpulence and anticancer.
- T. Hirata, Misato Fujii, Daiki Hongo
- Chemistry, MedicineBioorganic & Medicinal Chemistry
- 2009
Silk protein, sericin, suppresses DMBA-TPA-induced mouse skin tumorigenesis by reducing oxidative stress, inflammatory responses and endogenous tumor promoter TNF-alpha.
- Siqin Zhaorigetu, N. Yanaka, M. Sasaki, Hiromitsu Watanabe, N. Kato
- Biology, MedicineOncology Report
- 1 May 2003
The results suggest that sericin possesses protective effect against tumor promotion in mouse skin by suppressing oxidative stress, inflammatory responses and TNF-alpha.
A Novel Glycerophosphodiester Phosphodiesterase, GDE5, Controls Skeletal Muscle Development via a Non-enzymatic Mechanism*
- Yuri Okazaki, Noriyasu Ohshima, N. Yanaka
- BiologyJournal of Biological Chemistry
- 24 June 2010
Results indicate that GDE5 negatively regulates skeletal muscle development even without GroPCho phosphodiesterase activity, providing novel insight into the biological significance of mammalian GP-PDE function in a non-enzymatic mechanism.
The emerging physiological roles of the glycerophosphodiesterase family
- D. Corda, M. Mosca, Noriyasu Ohshima, L. Grauso, N. Yanaka, S. Mariggiò
- BiologyThe FEBS Journal
- 1 February 2014
GDE5 has been shown to inhibit skeletal muscle development independent of its enzymatic activity, indicating that mammalian glycerophosphodiesterases have high substrate specificities, even if the number of potential physiological substrates is continuously increasing.
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