Screening for the Preferred Substrate Sequence of Transglutaminase Using a Phage-displayed Peptide Library
- Y. Sugimura, Masayo Hosono, Fumitaka Wada, T. Yoshimura, M. Maki, K. Hitomi
- Biology, ChemistryJournal of Biological Chemistry
- 30 June 2006
The amino acid sequences that demonstrated higher specificity and inhibitory activity in the cross-linking reactions by TGase 2 and Factor XIIIa were identified and confirmed that the sequences were favored for transamidation using modified glutathione S-transferase (GST) for recombinant peptide-GST fusion proteins.
Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel…
- H. Mihara, T. Kurihara, T. Yoshimura, K. Soda, N. Esaki
- Biology, ChemistryJournal of Biological Chemistry
- 5 September 1997
The Escherichia coli genome contains three genes with sequence homology to nifS, and a new enzyme catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L- Cysteine sulfinate desulfinase, and L-selenocystine to produce L-alanine is named.
Crystal Structure of a Homolog of Mammalian Serine Racemase from Schizosaccharomyces pombe*
- M. Goto, T. Yamauchi, N. Esaki
- Chemistry, BiologyJournal of Biological Chemistry
- 28 July 2009
The crystal-soaking experiment showed that the substrate serine was actually trapped in the active site of the modified enzyme, suggesting that the lysino-d-alanyl residue acts as a catalytic base in the same manner as inherent Lys-57 of the wild-type enzyme.
Cold-Active Serine Alkaline Protease from the Psychrotrophic Bacterium Shewanella Strain Ac10: Gene Cloning and Enzyme Purification and Characterization
- L. Kulakova, A. Galkin, T. Kurihara, T. Yoshimura, N. Esaki
- BiologyApplied and Environmental Microbiology
- 1 February 1999
The recombinant SapSh (rSapSh) was found to have a molecular weight of about 44,000 and to be highly active in the alkaline region (optimum pH, around 9.0) when azocasein and synthetic peptides were used as substrates, but was far less stable than the subtilisin.
Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions.
- H. Mihara, T. Kurihara, T. Yoshimura, N. Esaki
- Biology, ChemistryJournal of Biochemistry (Tokyo)
- 1 April 2000
Three NifS homologs from Escherichia coli, CSD, CsdB, and IscS, that appear to be involved in iron-sulfur cluster formation and/or the biosynthesis of selenophosphate are purified, suggesting the presence of different rate-limiting steps or reaction mechanisms for L-cysteine desulfurization and the degradation of L-selenocysteine.
Synthesis of optically active amino acids from alpha-keto acids with Escherichia coli cells expressing heterologous genes
- A. Galkin, L. Kulakova, T. Yoshimura, K. Soda, N. Esaki
- Biology, EngineeringApplied and Environmental Microbiology
- 1 December 1997
A simple method for enzymatic synthesis of L and D amino acids from alpha-keto acids with Escherichia coli cells which express heterologous genes is described and optic pure D enantiomers of glutamate and leucine were obtained.
Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly
- Shin-ichiro Kato, H. Mihara, N. Esaki
- Chemistry, BiologyProceedings of the National Academy of Sciences…
- 23 April 2002
A mechanism for an early stage of iron-sulfur cluster assembly is proposed: the sulfur transfer from IscS to Isc U is initiated by the attack of Cys-63 of IscU on the Sγ atom of CYS-328 of IsCS that is bound to sulfane sulfur derived from l-cysteine.
Conserved Pyridoxal Protein That Regulates Ile and Val Metabolism
- Tomokazu Ito, Jumpei Iimori, T. Yoshimura
- BiologyJournal of Bacteriology
- 4 October 2013
It is demonstrated for the first time that YggS controls Ile and Val metabolism by modulating 2-ketobutyrate and CoA availability and fully reversed phenotypes conferred by the yggS mutation.
Serine racemase is involved in d-aspartate biosynthesis.
- Tomokazu Ito, Mika Hayashida, H. Mori
- BiologyJournal of Biochemistry (Tokyo)
- 1 December 2016
It is shown that mammalian serine racemase (SRR), the primary enzyme responsible for brain d-Ser production, catalyses Asp racemization via a two-base mechanism, and that SRR indeed acts as a d-Asp biosynthetic enzyme in some organs and/or tissues.
Reaction Mechanism of Alanine Racemase from Bacillus stearothermophilus
- A. Watanabe, T. Yoshimura, B. Mikami, H. Hayashi, H. Kagamiyama, N. Esaki
- Chemistry, BiologyJournal of Biological Chemistry
- 24 May 2002
A mechanism of alanine racemase reaction in which the substrate carboxyl group directly participates in the catalysis by mediating the proton transfer between the two catalytic bases, Lys39 and Tyr265′ is proposed.
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