Comparison of Acyl-CoA Synthetic Activities and Enantioselectivity toward 2-Arylpropanoic Acids in Firefly Luciferases
スポンサーリンク
概要
- 論文の詳細を見る
Measurement of thioesterification activities for dodecanoic acid (C12) and ketoprofen was done using five firefly luciferases, from Pyrocoelia miyako (PmL), Photinus pyralis (PpL), Luciola cruciata (LcL), Hotaria parvura (HpL), and Luciola mingrelica (LmL). Among these, PmL, PpL, and LcL showed the expected thioesterification activities toward both substrates. All the enzymes exhibited (R)-enantioselectivity toward ketoprofen, which had same tendency as firefly luciferase from Luciola lateralis (LUC-H). HpL and LmL, however, did not accept ketoprofen, although they had thioesterification activity toward C12. These results indicate that the substrate acceptance of luciferases for the thioesterification reaction varies dramatically relying on the origin of firefly. Hence we focused primarily on PmL and investigated the effect of pH on enzymatic activity. In addition, by determining the kinetic parameters at various pH values, we verified that the kcat parameter contributed to the preferential enantioselectivity of this enzyme.
著者
-
Negoro Seiji
Department Of Biotechnology Faculty Of Engineering Osaka University
-
Takeo Masahiro
Department Of Applied Chemistry Himeiji Institute Of Technology
-
Kato Dai-ichiro
Graduate School Of Engineering University Of Hyogo
-
Yoshida Hiromitsu
Graduate School Of Engineering University Of Hyogo
-
Kato Dai-ichiro
Department Of Materials Science And Chemistry Graduate School Of Engineering University Of Hyogo
-
YOKOYAMA Keisuke
Department of Materials Science and Chemistry, Graduate School of Engineering, University of Hyogo
-
HIRAISHI Yoshihiro
Department of Materials Science and Chemistry, Graduate School of Engineering, University of Hyogo
関連論文
- Enzyme-linked Immunosorbent Assay for Nonylphenol Using Antibody-Bound Microfluid Filters in Vertical Fluidic Operation(METHODS)
- Mutational Analysis of the Metabolism of 2,6-Naphthalenedisulfonate by Pigmentiphaga sp. NDS-2
- フロック形成菌Pigmentiphaga sp. NDS-1による2,6-ナフタレンジスルホン酸の生物分解
- Characterization of Hybrid Enzymes between 6-Aminohexanoate-Dimer Hydrolase and Its Analogous Protein
- Alteration of Catalytic Function of 6-Aminohexanoate-Dimer Hydrolase by Site-Directed Mutagenesis
- Molecular Cloning and Sequencing of the Phenol Hydroxylase Gene from Pseudomonas putida BH
- Expression of the Xylan-Degrading Genes of Bacillus pumilus IPO in Saccharomyces cerevisiae
- 1P042 Molecular dynamics studies on Mutational structures of a Nylon-6 Byproduct-degrading Enzyme(Protein:Structure & Function,The 48th Annual Meeting of the Biophysical Society of Japan)
- Construction and Characterization of N-Terminally Truncated DNA Polymerase from Thermus thermophilus
- Analysis of a Promoter-Like Region in Flavobacterium Which Controls 6-Aminohexanoic Acid Linear Oligomer Hydrolase Gene Expression in Escherichia coli
- Trichloroethylene Degradation by Genetically Engineered Bacteria Carrying Cloned Phenol Catabolic Genes
- Genetic Organization of Nylon-Oligomer-Degrading Enzymes from Alkalophilic Bacterium, Agromyces sp. KY5R(GENETICS, MOLECULAR BIOLOGY, AND GENE ENGINEERING)
- Purification and Characterization of Alkylcatechol 2,3-Dioxygenase from Butylphenol Degradation Pathway of Pseudomonas putida MT4(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Characterization of Alkylphenol Degradation Gene Cluster in Pseudomonas putida MT4 and Evidence of Oxidation of Alkylphenols and Alkylcatechols with Medium-Length Alkyl Chain(ENVIRONMENTAL BIOTECHNOLOGY)
- Characterization of Endo-Type 6-Aminohexanoate-Oligomer Hydrolase from Flavobacterium sp.
- Structure of Isozyme Genes of Glucose Dehydrogenase from Bacillus megaterium IAM1030
- Purification and Characterization of a New Glucose Dehydrogenase from Vegetative Cells of Bacillus megaterium
- Simultaneous Degradation of 4-Nitrophenol and Picric Acid by Two Different Mechanisms of Rhodococcus sp. PN1
- Cloning and Characterization of a 4-Nitrophenol Hydroxylase Gene Cluster from Rhodococcus sp. PN1
- Plasmid-Coded Degradation of Salicylate Using the Catechol Cleavage Pathway of the Host
- Mineralization and Desulfonation of 3-Nitrobenzenesulfonic Acid by Alcaligenes sp. GA-1
- Biodegradability of 3-Methyl-4-Nitrophenol by 4-Nitrophenol-Degrading Bacteria
- Purification and Gene Cloning of an Enantioselective Thioesterification Enzyme from Brevibacterium ketoglutamicum KU1073, a Deracemization Bacterium of 2-(4-Chlorophenoxy)propanoic Acid
- Immunoassay Using Microfluid Filters Constructed by Deep X-Ray Lithography
- Purification and Characterization of Catechol 2,3-Dioxygenase from the Aniline Degradation Pathway of Acinetobacter sp. YAA and Its Mutant Enzyme, Which Resists Substrate Inhibition
- Identification and characterization of another 4-nitrophenol degradation gene cluster, nps, in Rhodococcus sp. strain PN1(ENVIRONMENTAL BIOTECHNOLOGY)
- Comparison of Acyl-CoA Synthetic Activities and Enantioselectivity toward 2-Arylpropanoic Acids in Firefly Luciferases
- Comparison of Acyl-CoA Synthetic Activities and Enantioselectivity toward 2-Arylpropanoic Acids in Firefly Luciferases
- Physical Map of Nylon Oligomer Degradative Plasmid pOAD2 Harbored in Flavobacterium sp. KI72