scholarly journals Identification of amino acid residues essential for catalytic activity of gentisate 1,2-dioxygenase fromPseudomonas alcaligenesNCIB 9867

2001 ◽  
Vol 204 (1) ◽  
pp. 141-146 ◽  
Author(s):  
Chi Hung Chua ◽  
Yongmei Feng ◽  
Chew Chieng Yeo ◽  
Hoon Eng Khoo ◽  
Chit Laa Poh
2013 ◽  
Vol 98 (4) ◽  
pp. 1641-1649 ◽  
Author(s):  
Wenna Bao ◽  
Haifeng Pan ◽  
Zhenhong Zhang ◽  
Yongqing Cheng ◽  
Zhipeng Xie ◽  
...  

2006 ◽  
Vol 102 (4) ◽  
pp. 362-364 ◽  
Author(s):  
Shigekazu Yano ◽  
Aki Kamemura ◽  
Kazuaki Yoshimune ◽  
Mitsuaki Moriguchi ◽  
Sachiko Yamamoto ◽  
...  

2016 ◽  
Vol 60 (10) ◽  
pp. 6084-6090 ◽  
Author(s):  
Dandan He ◽  
Jiachi Chiou ◽  
Zhenling Zeng ◽  
Edward Wai-Chi Chan ◽  
Jian-Hua Liu ◽  
...  

ABSTRACTClinical isolates producing hybrid CTX-M β-lactamases, presumably due to recombination between theblaCTX-M-15andblaCTX-M-14elements, have emerged in recent years. Among the hybrid enzymes, CTX-M-64 and CTX-M-14 display the most significant difference in catalytic activity. This study aims to investigate the mechanisms underlying such differential enzymatic activities in order to provide insight into the structure/function relationship of this class of enzymes. Sequence alignment analysis showed that the major differences between the amino acid composition of CTX-M-64 and CTX-M-14 lie at both the N and C termini of the enzymes. Single or multiple amino acid substitutions introduced into CTX-M-64 and CTX-M-14 were found to produce only minor effects on hydrolytic functions; such a finding is consistent with the notion that the discrepancy between the functional activities of the two enzymes is not the result of only a few amino acid changes but is attributable to interactions between a unique set of amino acid residues in each enzyme. This theory is supported by the results of the thermal stability assay, which confirmed that CTX-M-64 is significantly more stable than CTX-M-14. Our data confirmed that, in addition to the important residues located in the active site, residues distal to the active site also contribute to the catalytic activity of the enzyme through stabilizing its structural integrity.


2005 ◽  
Vol 100 (5) ◽  
pp. 545-550 ◽  
Author(s):  
Makoto Shimosaka ◽  
Kazuaki Sato ◽  
Naohide Nishiwaki ◽  
Takashi Miyazawa ◽  
Mitsuo Okazaki

Sign in / Sign up

Export Citation Format

Share Document