Visualized characterization of bacterial penicillin G acylase for the hydrolysis of β-lactams using an activatable NIR fluorescent probe

2020 ◽  
Vol 310 ◽  
pp. 127872 ◽  
Author(s):  
Zhenhao Tian ◽  
Lei Feng ◽  
Lu Li ◽  
Xiangge Tian ◽  
Jingnan Cui ◽  
...  
Keyword(s):  
Fluorescent Probe ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Hydrolysis Of

scholarly journals <italic>In vivo</italic> imaging of penicillin G acylase in mice via a near-infrared fluorescent probe

2017 ◽  
Vol 47 (8) ◽  
pp. 994-999
Author(s):  
Xiaohua Li ◽  
Xinyuan He ◽  
Wen Shi ◽  
Haolin Zhang ◽  
Huimin Ma
Keyword(s):  
Fluorescent Probe ◽  
Near Infrared ◽  
Penicillin G Acylase ◽  
Penicillin G

scholarly journals Gold Nanoparticles for Colorimetric detection of hydrolysis of antibiotics by penicillin G acylase

2010 ◽  
Vol 01 (04) ◽  
pp. 322-329 ◽  
Author(s):  
Neha R. Tiwari ◽  
Ambrish Rathore ◽  
Asmita Prabhune ◽  
Sulabha K. Kulkarni
Keyword(s):  
Gold Nanoparticles ◽  
Colorimetric Detection ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Hydrolysis Of

Hydrolysis of Penicillin G by Penicillin G Acylase Immobilized on Chitosan Microbeads in Different Reactor Systems

2011 ◽  
Vol 34 (10) ◽  
pp. 1706-1714 ◽  
Author(s):  
M. G. Žuža ◽  
B. M. Obradović ◽  
Z. D. Knežević-Jugović
Keyword(s):  
Penicillin G Acylase ◽  
Penicillin G ◽  
Hydrolysis Of

Asymmetric hydrolysis of dimethyl phenylmalonate by immobilized penicillin G acylase from E. coli

2007 ◽  
Vol 40 (5) ◽  
pp. 997-1000 ◽  
Author(s):  
Zaida Cabrera ◽  
Fernando Lopez-Gallego ◽  
Gloria Fernandez-Lorente ◽  
Jose M. Palomo ◽  
Tamara Montes ◽  
...  
Keyword(s):  
Penicillin G Acylase ◽  
Penicillin G ◽  
E Coli ◽  
Immobilized Penicillin G Acylase ◽  
Hydrolysis Of

scholarly journals Rapid burst kinetics in the hydrolysis of 4-nitrophenyl acetate by penicillin G acylase from Kluyvera citrophila. Effects of mutation F360V on rate constants for acylation and de-acylation

1996 ◽  
Vol 316 (2) ◽  
pp. 409-412 ◽  
Author(s):  
A Roa ◽  
M L Goble ◽  
J L García ◽  
C Acebal ◽  
R Virden
Keyword(s):  
Rate Constants ◽  
Acetyl Derivative ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Side Chain ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Burst Kinetics ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetics of release of 4-nitrophenol were followed by stopped-flow spectrophotometry with two 4-nitrophenyl ester substrates of penicillin G acylase from Kluyvera citrophila. With the ester of acetic acid, but not of propionic acid, there was a pre-steady-state exponential phase, the kinetics of which were inhibited by phenylacetic acid (a product of hydrolysis of specific substrates) to the extent predicted from Ki values. This was interpreted as deriving from rapid formation (73 mM-1·s-1) and slow hydrolysis (0.76 s-1) of an acetyl derivative of the side chain of the catalytic-centre residue Ser-290. With the mutant F360V, which differs from the wild-type enzyme in its ability to hydrolyse adipyl-L-leucine and has a kcat for 4-nitrophenyl acetate one-twentieth that of the wild-type enzyme, the corresponding values for the rates of formation and hydrolysis of the acetyl-enzyme were 11.1 mM-1·s-1 and 0.051 s-1 respectively. The ratio of these rate constants was three times that for the wild-type enzyme, suggesting that the mutant is less impaired in the rate of formation of an acetyl-enzyme than in its subsequent hydrolysis.

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