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Alteration of coenzyme specificity of lactate dehydrogenase from Thermus thermophilus by introducing the loop region of NADP(H)-dependent malate dehydrogenase.
Biosci Biotechnol Biochem. 2006 Sep; 70(9):2230-5.BB

Abstract

Previously we found that replacement of seven amino acid residues in a loop region markedly shifted the coenzyme specificity of malate dehydrogenase from NAD(H) toward NADP(H). In the present study, we replaced the seven amino acid residues in the corresponding region of an NAD(H)-dependent lactate dehydrogenase with those of NADP(H)-dependent malate dehydrogenase, and examined the coenzyme specificity of the resulting mutant enzyme. Coenzyme specificity was significantly shifted by 399-fold toward NADPH when k cat/Km(coenzyme) was used as the measure of coenzyme specificity. The effect of the replacements on coenzyme specificity is discussed based on in silico simulation of the three-dimensional structure of the lactate dehydrogenase mutant.

Authors+Show Affiliations

Biotechnology Research Center, The University of Tokyo, Tokyo, Japan.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

16960374

Citation

Tomita, Takeo, et al. "Alteration of Coenzyme Specificity of Lactate Dehydrogenase From Thermus Thermophilus By Introducing the Loop Region of NADP(H)-dependent Malate Dehydrogenase." Bioscience, Biotechnology, and Biochemistry, vol. 70, no. 9, 2006, pp. 2230-5.
Tomita T, Kuzuyama T, Nishiyama M. Alteration of coenzyme specificity of lactate dehydrogenase from Thermus thermophilus by introducing the loop region of NADP(H)-dependent malate dehydrogenase. Biosci Biotechnol Biochem. 2006;70(9):2230-5.
Tomita, T., Kuzuyama, T., & Nishiyama, M. (2006). Alteration of coenzyme specificity of lactate dehydrogenase from Thermus thermophilus by introducing the loop region of NADP(H)-dependent malate dehydrogenase. Bioscience, Biotechnology, and Biochemistry, 70(9), 2230-5.
Tomita T, Kuzuyama T, Nishiyama M. Alteration of Coenzyme Specificity of Lactate Dehydrogenase From Thermus Thermophilus By Introducing the Loop Region of NADP(H)-dependent Malate Dehydrogenase. Biosci Biotechnol Biochem. 2006;70(9):2230-5. PubMed PMID: 16960374.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Alteration of coenzyme specificity of lactate dehydrogenase from Thermus thermophilus by introducing the loop region of NADP(H)-dependent malate dehydrogenase. AU - Tomita,Takeo, AU - Kuzuyama,Tomohisa, AU - Nishiyama,Makoto, Y1 - 2006/09/07/ PY - 2006/9/9/pubmed PY - 2006/12/9/medline PY - 2006/9/9/entrez SP - 2230 EP - 5 JF - Bioscience, biotechnology, and biochemistry JO - Biosci. Biotechnol. Biochem. VL - 70 IS - 9 N2 - Previously we found that replacement of seven amino acid residues in a loop region markedly shifted the coenzyme specificity of malate dehydrogenase from NAD(H) toward NADP(H). In the present study, we replaced the seven amino acid residues in the corresponding region of an NAD(H)-dependent lactate dehydrogenase with those of NADP(H)-dependent malate dehydrogenase, and examined the coenzyme specificity of the resulting mutant enzyme. Coenzyme specificity was significantly shifted by 399-fold toward NADPH when k cat/Km(coenzyme) was used as the measure of coenzyme specificity. The effect of the replacements on coenzyme specificity is discussed based on in silico simulation of the three-dimensional structure of the lactate dehydrogenase mutant. SN - 0916-8451 UR - https://www.unboundmedicine.com/medline/citation/16960374/Alteration_of_coenzyme_specificity_of_lactate_dehydrogenase_from_Thermus_thermophilus_by_introducing_the_loop_region_of_NADP_H__dependent_malate_dehydrogenase_ L2 - http://joi.jlc.jst.go.jp/JST.JSTAGE/bbb/60170?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -