penicillin v acylase
Recently Published Documents


TOTAL DOCUMENTS

48
(FIVE YEARS 1)

H-INDEX

12
(FIVE YEARS 0)

2021 ◽  
Vol 9 (4) ◽  
pp. 732
Author(s):  
Jack W. Daly ◽  
Stephen J. Keely ◽  
Cormac G. M. Gahan

Bile salt hydrolase (BSH) and penicillin V acylase (PVA) are related enzymes that are classified as choloylglycine hydrolases (CGH). BSH enzymes have attracted significant interest for their ability to modulate the composition of the bile acid pool, alter bile acid signaling events mediated by the host bile acid receptors FXR and TGR5 and influence cholesterol homeostasis in the host, while PVA enzymes have been widely utilised in an industrial capacity in the production of semi-synthetic antibiotics. The similarities between BSH and PVA enzymes suggest common evolution of these enzymes and shared mechanisms for substrate binding and catalysis. Here, we compare BSH and PVA through analysis of the distribution, phylogeny and biochemistry of these microbial enzymes. The development of new annotation approaches based upon functional enzyme analyses and the potential implications of BSH enzymes for host health are discussed.



ACS Omega ◽  
2020 ◽  
Vol 5 (45) ◽  
pp. 28972-28976
Author(s):  
Amol M. Sawant ◽  
Avinash Vellore Sunder ◽  
Koteswara Rao Vamkudoth ◽  
Sureshkumar Ramasamy ◽  
Archana Pundle






2016 ◽  
Vol 193 (2) ◽  
pp. 85-94 ◽  
Author(s):  
Vellore Sunder Avinash ◽  
Priyabrata Panigrahi ◽  
Deepak Chand ◽  
Archana Pundle ◽  
Cheravakattu Gopalan Suresh ◽  
...  






2014 ◽  
Vol 81 (4) ◽  
pp. 1225-1233 ◽  
Author(s):  
Jesús Torres-Bacete ◽  
Daniel Hormigo ◽  
Raquel Torres-Gúzman ◽  
Miguel Arroyo ◽  
María Pilar Castillón ◽  
...  

ABSTRACTThepvagene fromStreptomyces lavendulaeATCC 13664, encoding a novel penicillin V acylase (SlPVA), has been isolated and characterized. The gene encodes an inactive precursor protein containing a secretion signal peptide that is activated by two internal autoproteolytic cleavages that release a 25-amino-acid linker peptide and two large domains of 18.79 kDa (α-subunit) and 60.09 kDa (β-subunit). Based on sequence alignments and the three-dimensional model ofSlPVA, the enzyme contains a hydrophobic pocket involved in catalytic activity, including Serβ1, Hisβ23, Valβ70, and Asnβ272, which were confirmed by site-directed mutagenesis studies. The heterologous expression ofpvainS. lividansled to the production of an extracellularly homogeneous heterodimeric enzyme at a 5-fold higher concentration (959 IU/liter) than in the original host and in a considerably shorter time. According to the catalytic properties ofSlPVA, the enzyme must be classified as a new member of the Ntn-hydrolase superfamily, which belongs to a novel subfamily of acylases that recognize substrates with long hydrophobic acyl chains and have biotechnological applications in semisynthetic antifungal production.



2013 ◽  
Vol 437 (4) ◽  
pp. 538-543 ◽  
Author(s):  
V.S. Avinash ◽  
Priyabrata Panigrahi ◽  
C.G. Suresh ◽  
Archana V. Pundle ◽  
Sureshkumar Ramasamy




Sign in / Sign up

Export Citation Format

Share Document