Activation and Stabilization of Penicillin V Acylase from Streptomyces lavendulae in the Presence of Glycerol and Glycols

2000 ◽  
Vol 16 (3) ◽  
pp. 368-371 ◽  
Author(s):  
M. Arroyo ◽  
R. Torres-Guzman ◽  
I. de la Mata ◽  
M.P. Castillon ◽  
C. Acebal
Keyword(s):  
Penicillin V ◽  
Streptomyces Lavendulae ◽  
Penicillin V Acylase

Chemical mechanism of penicillin V acylase from Streptomyces lavendulae: pH-dependence of kinetic parameters

2001 ◽  
Vol 16 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Raquel Torres-Guzmán ◽  
Isabel de la Mata ◽  
Jesús Torres-Bacete ◽  
Miguel Arroyo ◽  
Marı́a Pilar Castillón ◽  
...  
Keyword(s):  
Kinetic Parameters ◽  
Ph Dependence ◽  
Chemical Mechanism ◽  
Penicillin V ◽  
Streptomyces Lavendulae ◽  
Penicillin V Acylase

Enhanced production of penicillin V acylase from Streptomyces lavendulae

1999 ◽  
Vol 53 (1) ◽  
pp. 81-84 ◽  
Author(s):  
R. Torres ◽  
F. Ramón ◽  
I. de la Mata ◽  
C. Acebal ◽  
M. P. Castillón
Keyword(s):  
Penicillin V ◽  
Streptomyces Lavendulae ◽  
Enhanced Production ◽  
Penicillin V Acylase

The Kinetic Mechanism of Penicillin V Acylase from Streptomyces Lavendulae

2001 ◽  
Vol 19 (4) ◽  
pp. 301-313 ◽  
Author(s):  
Raquel Torres-Guzmán ◽  
Isabel De La Mata ◽  
Miguel Arroyo ◽  
Jesús Torres-Bacete ◽  
M. Pilar Castillon ◽  
...  
Keyword(s):  
Kinetic Mechanism ◽  
Penicillin V ◽  
Streptomyces Lavendulae ◽  
Penicillin V Acylase

scholarly journals Overexpression of Penicillin V Acylase from Streptomyces lavendulae and Elucidation of Its Catalytic Residues

2014 ◽  
Vol 81 (4) ◽  
pp. 1225-1233 ◽  
Author(s):  
Jesús Torres-Bacete ◽  
Daniel Hormigo ◽  
Raquel Torres-Gúzman ◽  
Miguel Arroyo ◽  
María Pilar Castillón ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Site Directed Mutagenesis ◽  
Three Dimensional Model ◽  
Sequence Alignments ◽  
Α Subunit ◽  
Content Type ◽  
Penicillin V ◽  
Linker Peptide ◽  
Streptomyces Lavendulae ◽  
Penicillin V Acylase

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.

Structural modelling of substrate binding and inhibition in penicillin V acylase from Pectobacterium atrosepticum

2013 ◽  
Vol 437 (4) ◽  
pp. 538-543 ◽  
Author(s):  
V.S. Avinash ◽  
Priyabrata Panigrahi ◽  
C.G. Suresh ◽  
Archana V. Pundle ◽  
Sureshkumar Ramasamy
Keyword(s):  
Substrate Binding ◽  
Structural Modelling ◽  
Pectobacterium Atrosepticum ◽  
Penicillin V ◽  
Penicillin V Acylase
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