Site specific mutants of β-galactosidase show that Tyr-503 is unimportant in Mg2+ binding but that Glu-461 is very important and may be a ligand to Mg2+-Reference-Cited by-同舟云学术

Site specific mutants of β-galactosidase show that Tyr-503 is unimportant in Mg2+ binding but that Glu-461 is very important and may be a ligand to Mg2+

Published:1990-08 Issue:1 Volume:171 Page:33-37
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Edwards Robert A.,Cupples Claire G.,Huber Reuben E.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference23 articles.

1. Interaction of the lacZ β-galactosidase of Escherichia coli with some β-d-galactopyranoside competitive inhibitors

2. The role of magnesium ions in β-galactosidase-catalysed hydrolyses. Studies on charge and shape of the β-galactopyranosyl-binding site

3. pH Dependence of the Activity of beta-Galactosidase from Escherichia coli

4. Interaction of divalent cations with .beta.-galactosidase (Escherichia coli)

5. Site-directed mutagenic replacement of glu-461 with gln in β-galactosidase (E. coli): Evidence that glu-461 is important for activity

Cited by 26 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. The functional mutational landscape of the lacZ gene;iScience;2023-12

2. Direct and indirect roles of His-418 in metal binding and in the activity of β-galactosidase (E. coli);Protein Science;2009-06

3. β-Galactosidase (Escherichia coli) has a second catalytically important Mg2+ site;Biochemical and Biophysical Research Communications;2007-01

4. β-Galactosidases (Escherichia coli) with Double Substitutions Show That Tyr-503 Acts Independently of Glu-461 but Cooperatively with Glu-537;Journal of Protein Chemistry;2003-11

5. Beta-D-Galactopyranosyl Azide;Applied Biochemistry and Biotechnology;2003