Home LiteratureArticle Details
PMID: 2658216 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

From analysis to synthesis: new ligand binding sites on the lactate dehydrogenase framework. Part I.

Trends in biochemical sciences ·Vol. 14 ·No. 3 ·1989-03-00 ·Pages 101-5

Clarke AR, Atkinson T, Holbrook JJ

Abstract

In Part I of this article, the naturally evolved protein framework of lactate dehydrogenase is investigated by genetically introduced modifications which reveal the structural basis of its catalytic and substrate-binding properties. In Part II (to be published in the April issue of TIBS), this analytical information is exploited in the design of two modified forms of the enzyme; one which is specific for a new substrate and one which lacks allosteric regulation.

MeSH Terms
Binding Sites L-Lactate Dehydrogenase/biosynthesis,metabolism Ligands/metabolism Structure-Activity Relationship
Chemicals
Ligands L-Lactate Dehydrogenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Clarke A R
Atkinson T
Holbrook J J
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1989-03-00
Pages
101-5
Language
English
Region
England
NLM ID
7610674
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com