Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Vellore Sunder Avinash"'
Autor:
Sawant, Amol M., Vellore Sunder, Avinash, Vamkudoth, Koteswara Rao, Ramasamy, Sureshkumar, Pundle, Archana
Publikováno v:
ACS Omega; 6/25/2024, Vol. 9 Issue 25, p27754-27754, 1p
Publikováno v:
Current Microbiology. 74:1332-1336
The twin-arginine translocase (Tat) pathway is involved in the transport of folded proteins in bacteria, and has been implicated in virulence and pathogenesis. A simple but efficient assay based on the quantification of the exopolysaccharide colanic
Publikováno v:
Critical Reviews in Biotechnology. 36:303-316
It is of great importance to study the physiological roles of enzymes in nature; however, in some cases, it is not easily apparent. Penicillin acylases are pharmaceutically important enzymes that cleave the acyl side chains of penicillins, thus pavin
Publikováno v:
Preparative biochemistrybiotechnology. 47(1)
The production of 6-aminopenicillanic acid (6-APA) is a key step in the manufacture of semisynthetic antibiotics in the pharmaceutical industry. The penicillin G acylase from Escherichia coli has long been utilized for this purpose. However, the use
Autor:
Archana Pundle, C.G. Suresh, Deepak Chand, Priyabrata Panigrahi, Sureshkumar Ramasamy, Vellore Sunder Avinash
Publikováno v:
Journal of structural biology. 193(2)
Penicillin V acylases (PVA) catalyze the deacylation of the beta-lactam antibiotic phenoxymethylpenicillin (Pen V). They are members of the Ntn hydrolase family and possess an N-terminal cysteine as the main catalytic nucleophile residue. They form t
Publikováno v:
International journal of biological macromolecules. 79
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
Autor:
Sureshkumar Ramasamy, Priyabrata Panigrahi, Cheravakkattu G. Suresh, Vellore Sunder Avinash, Archana Pundle
Publikováno v:
Biochemical and biophysical research communications. 437(4)
Penicillin V acylases (PVAs) and bile salt hydrolases (BSHs) have considerable sequence and structural similarity; however, they vary significantly in their substrate specificity. We have identified a PVA from a Gram-negative organism, Pectobacterium
Publikováno v:
Annals of Microbiology; Sep2012, Vol. 62 Issue 3, p1287-1293, 7p
Autor:
Philem, Pushparani D.1 (AUTHOR), Yadav, Yashpal1 (AUTHOR), Vellore Sunder, Avinash1 (AUTHOR), Ghosh, Deepanjan1 (AUTHOR), Prabhune, Asmita1 (AUTHOR), Ramasamy, Sureshkumar1 (AUTHOR) s.ramasamy@ncl.res.in
Publikováno v:
Biochimie. Oct2020, Vol. 177, p108-116. 9p.