scholarly journals Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis

2018 ◽  
Vol 9 (32) ◽  
pp. 6692-6702 ◽  
Author(s):  
Andrés Espinoza-Cara ◽  
Ulises Zitare ◽  
Damián Alvarez-Paggi ◽  
Sebastián Klinke ◽  
Lisandro H. Otero ◽  
...  

Loop directed mutagenesis leads to a cupredoxin withthe strongest copper–thiolate bond known to date, high reduction potential and imidazole binding properties.

2019 ◽  
Vol 4 (7) ◽  
pp. 2211-2217 ◽  
Author(s):  
Cheng Han ◽  
Bing Wang ◽  
Chunzhi Wu ◽  
Shujin Shen ◽  
Xiaoshan Zhang ◽  
...  

1994 ◽  
Vol 301 (2) ◽  
pp. 477-483 ◽  
Author(s):  
J M Wilkin ◽  
A Dubus ◽  
B Joris ◽  
J M Frère

The side chains of residues Thr299 and Thr301 in the Streptomyces R61 DD-peptidase have been modified by site-directed mutagenesis. These amino acids are part of a beta-strand which forms a wall of the active-site cavity. Thr299 corresponds to the second residue of the Lys-Thr(Ser)-Gly triad, highly conserved in active-site beta-lactamases and penicillin-binding proteins (PBPs). Modification of Thr301 resulted only in minor alterations of the catalytic and penicillin-binding properties of the enzyme. No selective decrease of the rate of acylation was observed for any particular class of compounds. By contrast, the loss of the hydroxy group of the residue in position 299 yielded a seriously impaired enzyme. The rates of inactivation by penicillins were decreased 30-50-fold, whereas the reactions with cephalosporins were even more affected. The efficiency of hydrolysis against the peptide substrate was also seriously decreased. More surprisingly, the mutant was completely unable to catalyse transpeptidation reactions. The conservation of an hydroxylated residue in this position in PBPs is thus easily explained by these results.


1992 ◽  
Vol 5 (2) ◽  
pp. 177-184 ◽  
Author(s):  
Makoto Nishiyama ◽  
Junko Suzuki ◽  
Tatsuya Ohnuki ◽  
Hae Choon Chang ◽  
Sueharu Horinouchi ◽  
...  

2011 ◽  
Vol 50 (7) ◽  
pp. 2885-2896 ◽  
Author(s):  
Jason England ◽  
Erik R. Farquhar ◽  
Yisong Guo ◽  
Matthew A. Cranswick ◽  
Kallol Ray ◽  
...  

2020 ◽  
Vol 44 (34) ◽  
pp. 14401-14410
Author(s):  
Chinmaya R. Mirle ◽  
Raja M. ◽  
Vasudevarao P. ◽  
Sankararaman S. ◽  
Kothandaraman R.

Prospective high reduction potential cathode materials have been proposed that can be used in non-aqueous redox flow battery applications.


2008 ◽  
Vol 190 (11) ◽  
pp. 3793-3798 ◽  
Author(s):  
Efthalia Kalliri ◽  
Scott B. Mulrooney ◽  
Robert P. Hausinger

ABSTRACT YgaF, a protein of previously unknown function in Escherichia coli, was shown to possess noncovalently bound flavin adenine dinucleotide and to exhibit l-2-hydroxyglutarate oxidase activity. The inability of anaerobic, reduced enzyme to reverse the reaction by reducing the product α-ketoglutaric acid is explained by the very high reduction potential (+19 mV) of the bound cofactor. The likely role of this enzyme in the cell is to recover α-ketoglutarate mistakenly reduced by other enzymes or formed during growth on propionate. On the basis of the identified function, we propose that this gene be renamed lhgO.


2015 ◽  
Vol 22 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Run-sheng Xu ◽  
Jian-liang Zhang ◽  
Hai-bin Zuo ◽  
Ke-xin Jiao ◽  
Zheng-wen Hu ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document