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Enhancement of the turnover number of thermostable malate dehydrogenase by deleting hydrogen bonds around the catalytic site.
Biochem Biophys Res Commun. 1996 Aug 23; 225(3):844-8.BB

Abstract

In malate dehydrogenase from Thermus flavus, substitution of Ile for Thr189, which is involved in hydrogen-bond network around a loop containing catalytic His186, caused an increase in the turnover number at room temperatures. In order to examine the effect of disruption of the hydrogen bonds on the catalytic activity, residues participating in the network were replaced by others which cannot form hydrogen bond by site-directed mutagenesis. All the mutations caused increases in the turnover number at room temperatures. This result suggests that an increase in flexibility introduced around catalytic site enhanced the catalytic activity of the malate dehydrogenase.

Authors+Show Affiliations

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

Pub Type(s)

Journal Article

Language

eng

PubMed ID

8780700

Citation

Nishiyama, M, et al. "Enhancement of the Turnover Number of Thermostable Malate Dehydrogenase By Deleting Hydrogen Bonds Around the Catalytic Site." Biochemical and Biophysical Research Communications, vol. 225, no. 3, 1996, pp. 844-8.
Nishiyama M, Kinoshita M, Kudo H, et al. Enhancement of the turnover number of thermostable malate dehydrogenase by deleting hydrogen bonds around the catalytic site. Biochem Biophys Res Commun. 1996;225(3):844-8.
Nishiyama, M., Kinoshita, M., Kudo, H., Horinouchi, S., & Tanokura, M. (1996). Enhancement of the turnover number of thermostable malate dehydrogenase by deleting hydrogen bonds around the catalytic site. Biochemical and Biophysical Research Communications, 225(3), 844-8.
Nishiyama M, et al. Enhancement of the Turnover Number of Thermostable Malate Dehydrogenase By Deleting Hydrogen Bonds Around the Catalytic Site. Biochem Biophys Res Commun. 1996 Aug 23;225(3):844-8. PubMed PMID: 8780700.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Enhancement of the turnover number of thermostable malate dehydrogenase by deleting hydrogen bonds around the catalytic site. AU - Nishiyama,M, AU - Kinoshita,M, AU - Kudo,H, AU - Horinouchi,S, AU - Tanokura,M, PY - 1996/8/23/pubmed PY - 1996/8/23/medline PY - 1996/8/23/entrez SP - 844 EP - 8 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 225 IS - 3 N2 - In malate dehydrogenase from Thermus flavus, substitution of Ile for Thr189, which is involved in hydrogen-bond network around a loop containing catalytic His186, caused an increase in the turnover number at room temperatures. In order to examine the effect of disruption of the hydrogen bonds on the catalytic activity, residues participating in the network were replaced by others which cannot form hydrogen bond by site-directed mutagenesis. All the mutations caused increases in the turnover number at room temperatures. This result suggests that an increase in flexibility introduced around catalytic site enhanced the catalytic activity of the malate dehydrogenase. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/8780700/Enhancement_of_the_turnover_number_of_thermostable_malate_dehydrogenase_by_deleting_hydrogen_bonds_around_the_catalytic_site_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(96)91261-9 DB - PRIME DP - Unbound Medicine ER -