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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Avinash, V. S. Ramasamy, Sureshkumar Suresh, C. G. Pundle, Archana |
| Description | Country affiliation: India Author Affiliation: Avinash VS ( Biochemical Sciences Division, National Chemical Laboratory, Dr Homi Bhabha road, Pune - 411008, India.); Ramasamy S ( Biochemical Sciences Division, National Chemical Laboratory, Dr Homi Bhabha road, Pune - 411008, India.); Suresh CG ( Biochemical Sciences Division, National Chemical Laboratory, Dr Homi Bhabha road, Pune - 411008, India.); Pundle A ( Biochemical Sciences Division, National Chemical Laboratory, Dr Homi Bhabha road, Pune - 411008, India. Electronic address: av.pundle@ncl.res.in.) |
| Abstract | Penicillin V acylases (PVAs, E.C.3.5.11) belong to the Ntn hydrolase super family of enzymes that catalyze the deacylation of the side chain from phenoxymethyl penicillin (penicillin V). Penicillin acylases find use in the pharmaceutical industry for the production of semi-synthetic antibiotics. PVAs employ the N-terminal cysteine residue as catalytic nucleophile and are structurally and evolutionarily related to bile salt hydrolases (BSHs). Here, we report the cloning and characterization of a PVA enzyme from the Gram-negative plant pathogen, Pectobacterium atrosepticum (PaPVA). The enzyme was cloned and expressed in Escherichia coli attaining a very high yield (250 mg/l) and a comparatively high specific activity (430 IU/mg). The enzyme showed marginally better pH and thermo-stability over PVAs characterized from Gram-positive bacteria. The enzyme also showed enhanced activity in presence of organic solvents and detergents. The enzyme kinetics turned out to be significantly different from that of previously reported PVAs, displaying positive cooperativity and substrate inhibition. The presence of bile salts had a modulating effect on PaPVA activity. Sequence analysis and characterization reveal the distinctive nature of these enzymes and underscore the need to study PVAs from Gram-negative bacteria. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 79 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-08-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Bacterial Proteins Chemistry Pectobacterium Penicillin Amidase Penicillin V Amidohydrolases Genetics Bile Acids And Salts Catalytic Domain Cloning, Molecular Escherichia Coli Metabolism Gene Expression Hydrogen-ion Concentration Kinetics Growth & Development Recombinant Proteins Sequence Analysis, Dna Substrate Specificity Temperature Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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