H
Hidenobu Komeda
Researcher at Toyama Prefectural University
Publications - 35
Citations - 786
Hidenobu Komeda is an academic researcher from Toyama Prefectural University. The author has contributed to research in topics: Amidase & Amino acid. The author has an hindex of 17, co-authored 35 publications receiving 736 citations.
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Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3.
Hidenobu Komeda,Yasuhisa Asano +1 more
TL;DR: The gene encoding the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3 was cloned and sequenced and the daaA gene modified in the nucleotide sequence upstream from its start codon was overexpressed in Escherichia coli.
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A gene cluster responsible for alkylaldoxime metabolism coexisting with nitrile hydratase and amidase in Rhodococcus globerulus A-4.
TL;DR: The existence of an aldoxime dehydratase genetically linked with NHase and amidase, and responsible for the metabolism of alkylaldoxime in R. globerulus is reported here.
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New Enzymatic Method of Chiral Amino Acid Synthesis by Dynamic Kinetic Resolution of Amino Acid Amides: Use of Stereoselective Amino Acid Amidases in the Presence of α-Amino-ε-Caprolactam Racemase
TL;DR: D- and l-amino acids were produced from l- and d-aminos acid amides by d-aminopeptidase from Ochrobactrum anthropi C1-38 and l -amino acid amidase from Pseudomonas azotoformans IAM 1603 by dynamic kinetic resolution of amino acid amide.
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A novel R‐stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine‐2‐tert‐butylcarboxamide
TL;DR: A novel amidase acting on (R,S)-piperazine-2-tert-butylcarboxamide was purified from Pseudomonas sp.
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Enhancement of the thermostability and catalytic activity of d-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3 by directed evolution
TL;DR: This work screened for the enzyme variants with improved thermostability generated by a directed evolution method with the goal of the application of evolved enzyme to the production of d-amino acids and obtained the most thermostable mutant BFB40, which was purified from the Escherichia coli (E. coli) transformant.