scholarly journals Kinetic characterization of a cocaine hydrolase engineered from mouse butyrylcholinesterase

2015 ◽  
Vol 466 (2) ◽  
pp. 243-251 ◽  
Author(s):  
Xiabin Chen ◽  
Xiaoqin Huang ◽  
Liyi Geng ◽  
Liu Xue ◽  
Shurong Hou ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Inhibition ◽  
Kinetic Characterization ◽  
Substrate Activation ◽  
Amino Acid Mutations ◽  
Human Butyrylcholinesterase

Mouse (mBChE) and human butyrylcholinesterase (hBChE)-based cocaine hydrolases (mCocH and hCocH) have remarkably different catalytic efficiencies against cocaine, but with little differences in catalytic efficiencies against acetylcholine (ACh) and butyrylthiocholine (BTC). The amino-acid mutations have remarkably converted substrate activation of the enzymes into substrate inhibition.

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases

Effect of Substrate Inhibition and Cooperativity on the Electrochemical Responses of Glucose Dehydrogenase. Kinetic Characterization of Wild and Mutant Types

2011 ◽  
Vol 133 (32) ◽  
pp. 12801-12809 ◽  
Author(s):  
Fabien Durand ◽  
Benoît Limoges ◽  
Nicolas Mano ◽  
François Mavré ◽  
Rebeca Miranda-Castro ◽  
...  
Keyword(s):  
Glucose Dehydrogenase ◽  
Substrate Inhibition ◽  
Kinetic Characterization

scholarly journals Kinetic characterization of high-activity mutants of human butyrylcholinesterase for the cocaine metabolite norcocaine

2013 ◽  
Vol 457 (1) ◽  
pp. 197-206 ◽  
Author(s):  
Max Zhan ◽  
Shurong Hou ◽  
Chang-Guo Zhan ◽  
Fang Zheng
Keyword(s):  
High Activity ◽  
Kinetic Modelling ◽  
Kinetic Characterization ◽  
In Vivo Tests ◽  
Human Butyrylcholinesterase

Catalytic parameters of butyrylcholinesterase and its mutants against norcocaine have been characterized in comparison with those against cocaine, indicating that the mutants can efficiently metabolize norcocaine, in addition to cocaine. Further in vivo tests and kinetic modelling support the indication.

Characterization of human tissuetype plasminogen activator variants with amino acid mutations in the kringle 1 domain

1992 ◽  
Vol 3 (4) ◽  
pp. 381-387 ◽  
Author(s):  
Y. Ikenaka ◽  
K. Yajima ◽  
H. Yahara ◽  
H. Maruyama ◽  
K. Matsumoto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Plasminogen Activator ◽  
Amino Acid Mutations

scholarly journals Analysis of Amino Acid Residues Involved in Catalysis of Polyethylene Glycol Dehydrogenase from Sphingopyxis terrae, Using Three-Dimensional Molecular Modeling-Based Kinetic Characterization of Mutants

2006 ◽  
Vol 72 (6) ◽  
pp. 4388-4396 ◽  
Author(s):  
Takeshi Ohta ◽  
Takeshi Kawabata ◽  
Ken Nishikawa ◽  
Akio Tani ◽  
Kazuhide Kimbara ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Amino Acid ◽  
Molecular Modeling ◽  
Binding Site ◽  
Active Sites ◽  
Substrate Binding ◽  
Three Dimensional ◽  
Kinetic Characterization ◽  
Amino Acid Residues

ABSTRACT Polyethylene glycol dehydrogenase (PEGDH) from Sphingopyxis terrae (formerly Sphingomonas terrae) is composed of 535 amino acid residues and one flavin adenine dinucleotide per monomer protein in a homodimeric structure. Its amino acid sequence shows 28.5 to 30.5% identity with glucose oxidases from Aspergillus niger and Penicillium amagasakiense. The ADP-binding site and the signature 1 and 2 consensus sequences of glucose-methanol-choline oxidoreductases are present in PEGDH. Based on three-dimensional molecular modeling and kinetic characterization of wild-type PEGDH and mutant PEGDHs constructed by site-directed mutagenesis, residues potentially involved in catalysis and substrate binding were found in the vicinity of the flavin ring. The catalytically important active sites were assigned to His-467 and Asn-511. One disulfide bridge between Cys-379 and Cys-382 existed in PEGDH and seemed to play roles in both substrate binding and electron mediation. The Cys-297 mutant showed decreased activity, suggesting the residue's importance in both substrate binding and electron mediation, as well as Cys-379 and Cys-382. PEGDH also contains a motif of a ubiquinone-binding site, and coenzyme Q10 was utilized as an electron acceptor. Thus, we propose several important amino acid residues involved in the electron transfer pathway from the substrate to ubiquinone.

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