Molecular modelling of CYP3A4 from an alignment with CYP102: Identification of key interactions between putative active site residues and CYP3A-specific chemicals

Xenobiotica ◽  
1996 ◽  
Vol 26 (10) ◽  
pp. 1067-1086 ◽  
Author(s):  
D. F. V. Lewis ◽  
P. J. Eddershaw ◽  
P. S. Goldfarb ◽  
M. H. Tarbit
Keyword(s):  
Molecular Modelling ◽  
Active Site ◽  
Active Site Residues ◽  
Putative Active Site

Identification of Putative Active-site Residues in the DNase Domain of Colicin E9 by Random Mutagenesis

1996 ◽  
Vol 260 (5) ◽  
pp. 731-742 ◽  
Author(s):  
Carole Garinot-Schneider ◽  
Ansgar J. Pommer ◽  
Geoffrey R. Moore ◽  
Colin Kleanthous ◽  
Richard James
Keyword(s):  
Active Site ◽  
Random Mutagenesis ◽  
Active Site Residues ◽  
Putative Active Site ◽  
Colicin E9

Analysis of putative active site residues of the poliovirus 3C protease

Virology ◽  
1991 ◽  
Vol 181 (2) ◽  
pp. 609-619 ◽  
Author(s):  
Katherine M. Kean ◽  
Natalya L. Teterina ◽  
Daniel Marc ◽  
Marc Girard
Keyword(s):  
Active Site ◽  
Active Site Residues ◽  
3C Protease ◽  
Putative Active Site

scholarly journals The histone H3-H4 tetramer is a copper reductase enzyme

Science ◽  
2020 ◽  
Vol 369 (6499) ◽  
pp. 59-64 ◽  
Author(s):  
Narsis Attar ◽  
Oscar A. Campos ◽  
Maria Vogelauer ◽  
Chen Cheng ◽  
Yong Xue ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Active Site ◽  
Histone H3 ◽  
Copper Binding ◽  
Active Site Residues ◽  
Chromatin Compaction ◽  
Putative Active Site ◽  
Dimerization Interface ◽  
Cellular Copper

Eukaryotic histone H3-H4 tetramers contain a putative copper (Cu2+) binding site at the H3-H3′ dimerization interface with unknown function. The coincident emergence of eukaryotes with global oxygenation, which challenged cellular copper utilization, raised the possibility that histones may function in cellular copper homeostasis. We report that the recombinant Xenopus laevis H3-H4 tetramer is an oxidoreductase enzyme that binds Cu2+ and catalyzes its reduction to Cu1+ in vitro. Loss- and gain-of-function mutations of the putative active site residues correspondingly altered copper binding and the enzymatic activity, as well as intracellular Cu1+ abundance and copper-dependent mitochondrial respiration and Sod1 function in the yeast Saccharomyces cerevisiae. The histone H3-H4 tetramer, therefore, has a role other than chromatin compaction or epigenetic regulation and generates biousable Cu1+ ions in eukaryotes.

scholarly journals Identification of putative active site residues of ACAT enzymes

2008 ◽  
Vol 49 (8) ◽  
pp. 1770-1781 ◽  
Author(s):  
Akash Das ◽  
Matthew A. Davis ◽  
Lawrence L. Rudel
Keyword(s):  
Active Site ◽  
Active Site Residues ◽  
Putative Active Site

scholarly journals Investigating the roles of putative active site residues in the oxalate decarboxylase from Bacillus subtilis

2007 ◽  
Vol 464 (1) ◽  
pp. 36-47 ◽  
Author(s):  
Draženka Svedružić ◽  
Yong Liu ◽  
Laurie A. Reinhardt ◽  
Ewa Wroclawska ◽  
W. Wallace Cleland ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Active Site ◽  
Active Site Residues ◽  
Oxalate Decarboxylase ◽  
Putative Active Site
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