Linked Life Data

7362828

Source:http://linkedlifedata.com/resource/pubmed/id/7362828

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-6-16
pubmed:abstractText
After solubilisation with urea and the non-ionic detergent Genapol X-100, the membrane-bound DD-carboxypeptidase (UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase, EC 3.4.12.6) of Bacillus coagulans NCIB 9365 was purified to homogeneity, as verified by sodium dodecyl sulphate gel electrophoresis, by chromatography with an ampicillin-agarose affinity resin and DEAE-cellulose. The properties of the purified DD-carboxypeptidase were similar to those of the membrane-bound enzyme; these include enhancement of activity by divalent cations, Pb2+ and Cd2+ being the most effective. The enzyme also catalysed a simple unnatural model transpeptidation reaction between UDP-N-acetylmuramoyl pentapeptide (donor) and D-alanine or glycine (acceptors). The enzyme consisted of a single polypeptide chain with a molecular weight (Mr 29 000), considerably lower than values obtained previously for most other DD-carboxypeptidases. However, its molecular weight and its degree of relatedness, as assessed by amino acid composition, were similar to several beta-lactamases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
612
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
107-18
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Purification and properties of the D-alanyl-D-alanine carboxypeptidase of Bacillus coagulans NCIB 9365.
pubmed:publicationType
Journal Article