CORE
🇺🇦
make metadata, not war
Services
Services overview
Explore all CORE services
Access to raw data
API
Dataset
FastSync
Content discovery
Recommender
Discovery
OAI identifiers
OAI Resolver
Managing content
Dashboard
Bespoke contracts
Consultancy services
Support us
Support us
Membership
Sponsorship
Community governance
Advisory Board
Board of supporters
Research network
About
About us
Our mission
Team
Blog
FAQs
Contact us
LysA2, the Lactobacillus casei bacteriophage A2 lysin is an endopeptidase active on a wide spectrum of lactic acid bacteria
Authors
Pedro Ribelles
Isabel Rodríguez
Juan Evaristo Suárez Fernández
Publication date
26 August 2013
Publisher
'Springer Science and Business Media LLC'
Doi
Cite
Abstract
The lysin gene (lysA2) of the Lactobacillus casei bacteriophage A2 was cloned and expressed in Escherichia coli. LysA2 is an endopeptidase that hydrolyzes the bond between the terminal d-alanine of the peptidoglycan tetrapeptide and the aspartic acid residue that forms the bridge with the l-lysine of a neighboring peptidoglycan chain, characteristic of Gram-positive bacteria included into the A4 peptidoglycan subgroup. This includes most lactobacilli, Lactococcus lactis, Pediococcus acidilactici, and Pediococcus pentosaceus, the walls of all of which were substrates for the enzyme. Specific binding of LysA2 to the wall of these bacteria is mediated by its C-terminal moiety, does not need the N-terminal catalytic domain for recognition, and is stable: at least 88% of the molecules were still bound to L. casei after 3 days in phosphate buffer at 4°C. The enzyme acts as a monomer, is active at pH values between 4 and 6, and at temperatures ranging between 18°C and 50°C while being independent of divalent cation addition. The enzyme showed strong resistance to incubation at high and low pH values but became progressively inactivated at 50°C and above. LysA2 is bactericidal, the viability of L. casei cultures dropping to 1% in 10 min, under the standard conditions used for the enzymatic assay. © 2011 Springer-Verlag.This work was supported by the CICYT grants BFU2007-65781 and AGL2010-15097 from the Ministry of Science and Technology (Spain) and the FEDER Plan.Peer Reviewe
Similar works
Full text
Available Versions
Digital.CSIC
See this paper in CORE
Go to the repository landing page
Download from data provider
oai:digital.csic.es:10261/8102...
Last time updated on 25/05/2016