Effects of substitution of Thr63 by alanine on the structure and function of Lactobacillus casei dihydrofolate reductase-Reference-Cited by-同舟云学术

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Effects of substitution of Thr63 by alanine on the structure and function of Lactobacillus casei dihydrofolate reductase

Published:1994 Issue:6 Volume:7 Page:783-792
ISSN:1741-0126
Container-title:"Protein Engineering, Design and Selection"
language:en
Short-container-title:Protein Eng Des Sel

Author:

Thomas Janette A.,Arnold John R.P.,Basran Jaswir,Andrews Julie,Roberts Gordon C.K.,Birdsall Berry,Feeney James

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/7/6/783/4242866/7-6-783.pdf

Cited by 8 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Improving the NADH-cofactor specificity of the highly active AdhZ3 and AdhZ2 from Escherichia coli K-12;Journal of Biotechnology;2014-11

2. Crystal structure of the non-regulatory A 4 isoform of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase complexed with NADP 1 1Edited by R. Huber;Journal of Molecular Biology;2001-11

3. Effects of single-residue substitutions on negative cooperativity in ligand binding to dihydrofolate reductase;Protein Engineering Design and Selection;1997-07-01

4. A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+;Journal of Molecular Biology;1997-05

5. Site-Directed Mutagenesis of a Serine Residue in Cinnamyl Alcohol Dehydrogenase, a Plant NADPH-Dependent Dehydrogenase, Affects the Specificity for the Coenzyme;Biochemistry;1995-09-26

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