A New Family of D-2-Hydroxyacid Dehydrogenases That Comprises D-Mandelate Dehydrogenases and 2-Ketopantoate Reductases
スポンサーリンク
概要
- 論文の詳細を見る
The gene for the D-mandelate dehydrogenase (D-ManDH) of Enterococcus faecalis IAM10071 was isolated by means of an activity staining procedure and PCR and expressed in Escherichia coli cells. The recombinant enzyme exhibited high catalytic activity toward various 2-ketoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-ketoisovalerate, and strict coenzyme specificity for NADH and NAD+. It showed marked sequence similarity with known NADP-dependent 2-ketopantoate reductases (KPR). These results indicate that together with KPR, D-ManDH constitutes a new family of D-2-hydroxyacid dehydrogenases that act on C3-branched 2-ketoacid substrates with various specificities for coenzymes and substrates.
- 社団法人 日本農芸化学会の論文
- 2008-04-23
著者
-
Taguchi Hayao
Department of Agricultural Chemistry, The University of Tokyo
-
SHINODA TAKESHI
Department of Materials Processing Engineering, Nagoya University
-
Tamura Yusuke
Department Of Applied Biological Science Faculty Of Science And Technology Tokyo University Of Scien
-
Ando Tomonori
Department Of Applied Biological Science Faculty Of Science And Technology Tokyo University Of Scien
-
WADA Yusuke
Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Sci
-
IWAI Saho
Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Sci
-
ARAI Kazuhito
Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Sci
-
Shinoda Takeshi
Department Of Applied Biological Science Faculty Of Science And Technology Tokyo University Of Scien
-
Shinoda Takeshi
Department Of Applied Biological Science Faculty Of Science And Technology Science University Of Tok
-
Iwai Saho
Department Of Applied Biological Science Faculty Of Science And Technology Tokyo University Of Scien
-
Wada Yusuke
Department Of Applied Biological Science Faculty Of Science And Technology Tokyo University Of Scien
-
Arai Kazuhito
Department Of Applied Biological Science Faculty Of Science And Technology Tokyo University Of Scien
-
Taguchi Hayao
Department Of Applied Biological Science Faculty Of Science And Technology Tokyo University Of Scien
関連論文
- TiAl Surface Coating on Titanium by Plasma Transferred Arc Surfacing and Its Oxidation Behavior
- Carboxypeptidase Taq, a Thermostable Zinc Enzyme, from Thermus aquaticus YT-1 : Molecular Cloning, Sequencing, and Expression of the Encoding Gene in Escherichia coli
- Purification and Characterization of a Thermostable Carboxypeptidase (Carboxypeptidase Taq) from Thermus aquaticus YT-1
- Physical characteristics of a new synthetic fiber mattress in relation to pressure sores
- Stability of Morphine Hydrochloride in a Total Parenteral Nutrient Solution
- Surface Modification by Friction Coating under Water
- A Methodology of Evaluation and Decision Making for Uncertainty Problems
- Involvement of Glu-264 and Arg-235 in the Essential Interaction between the Catalytic Imidazole and Substrate for the D-Lactate Dehydrogenase Catalysis
- A New Family of D-2-Hydroxyacid Dehydrogenases That Comprises D-Mandelate Dehydrogenases and 2-Ketopantoate Reductases
- Role of Histidine 188 in Fructose 1,6-Bisphosphate- and Divalent Cation-Regulated L-Lactate Dehydrogenase of Lactobacillus casei
- 13. Establishing the Evaluation and Decision Making Methods for Uncertainty Problems
- Recognition Site for the Side Chain of 2-Ketoacid Substrate in D-Lactate Dehydrogenase
- Cloning, Nucleotide Sequencing, and Expression in Escherichia coli of the Gene for Formate Dehydrogenase of Paracoccus sp. 12-A, a Formate-assimilating Bacterium(Biochemistry & Molecular Biology)
- Chewing Pattern Classification in Skeletal Class III Malocclusions
- A molecular design that stabilizes active state in bacterial allosteric L-lactate dehydrogenases
- Allosteric and Kinetic Properties of L-Lactate Dehydrogenase from Thermus caldophilus GK24, an Extremely Thermophilic Bacterium