scholarly journals Kinetic Characterization of Hydrolysis of Nitrocefin, Cefoxitin, and Meropenem by β-Lactamase from Mycobacterium tuberculosis

Biochemistry ◽  
2013 ◽  
Vol 52 (23) ◽  
pp. 4097-4104 ◽  
Author(s):  
Carmen Chow ◽  
Hua Xu ◽  
John S. Blanchard
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Kinetic Characterization ◽  
Hydrolysis Of

Kinetic characterization of hydrolysis of camel and bovine milk proteins by pancreatic enzymes

2008 ◽  
Vol 18 (12) ◽  
pp. 1097-1102 ◽  
Author(s):  
Maryam Salami ◽  
Reza Yousefi ◽  
Mohammad Reza Ehsani ◽  
Michèle Dalgalarrondo ◽  
Jean-Marc Chobert ◽  
...  
Keyword(s):  
Bovine Milk ◽  
Milk Proteins ◽  
Pancreatic Enzymes ◽  
Kinetic Characterization ◽  
Hydrolysis Of ◽  
Bovine Milk Proteins

scholarly journals Kinetic characterization of the acyl-enzyme mechanism for β-lactamase I

1988 ◽  
Vol 254 (3) ◽  
pp. 923-925 ◽  
Author(s):  
M T Martin ◽  
S G Waley
Keyword(s):  
Steady State ◽  
Rate Constants ◽  
Enzyme Mechanism ◽  
Beta Lactamase ◽  
Kinetic Characterization ◽  
Hydrolysis Of

beta-Lactamase I catalyses the hydrolysis of penicillins by an acyl-enzyme mechanism. A procedure was developed for determining the rate constants for the acylation and deacylation steps for the good substrates benzylpenicillin and phenoxymethylpenicillin; this depends on determining the fraction of enzyme that is present as acyl-enzyme in the steady state.

scholarly journals Spectral and kinetic characterization of 7,8-diaminopelargonic acid synthase from Mycobacterium tuberculosis

IUBMB Life ◽  
2006 ◽  
Vol 58 (4) ◽  
pp. 225-233 ◽  
Author(s):  
Vikrant Bhor ◽  
Sagarika Dev ◽  
Ganga Vasanthakumar ◽  
Avadhesha Surolia
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Kinetic Characterization

scholarly journals Mutational effects on carbapenem hydrolysis of YEM-1, a new sub-class B2 metallo-β-lactamase from Yersinia mollaretii

2020 ◽  
Author(s):  
P. S. Mercuri ◽  
R. Esposito ◽  
S. Blétard ◽  
S. Di Costanzo ◽  
M. Perilli ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Catalytic Efficiency ◽  
The Other ◽  
Kinetic Characterization ◽  
Activity Profile ◽  
Gene Coding ◽  
Hydrolysis Of

ABSTRACTThe analysis of the genome sequence of Yersinia mollaretii (Y. mollaretii) ATCC 43969 indicates the presence of the blaYEM gene coding for YEM-1, a putative subclass B2 metallo-β-lactamase. The objectives of our work were to produce, purify and complete the kinetic characterization of YEM-1. Compared to the known subclass B2 metallo–β-lactamases, YEM-1 displayed a narrowest substrate profile since it is only able to hydrolyse imipenem with a high catalytic efficiency but not all the other carbapenems tested such as biapenem, meropenem, doripenem and ertapenem. A possible explanation of this peculiar activity profile is the presence of tyrosine 67 (loop L1), threonine 156 (loop L2) and serine 236 (loop L3) respectively. We showed that the substitution of Y67 broadened the activity profile of the enzyme for all carbapenems but still displayed a poor activity toward the other β-lactam classes.

scholarly journals Kinetic characterization of human butyrylcholinesterase mutants for the hydrolysis of cocaethylene

2014 ◽  
Vol 460 (3) ◽  
pp. 447-457 ◽  
Author(s):  
Shurong Hou ◽  
Max Zhan ◽  
Xirong Zheng ◽  
Chang-Guo Zhan ◽  
Fang Zheng
Keyword(s):  
Kinetic Modelling ◽  
Kinetic Characterization ◽  
In Vivo Tests ◽  
Hydrolysis Of ◽  
Human Butyrylcholinesterase

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

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