Linked Life Data

21082226

Source:http://linkedlifedata.com/resource/pubmed/id/21082226

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2010-11-29
pubmed:abstractText
We previously isolated Streptomyces racemochromogenes strain 10-3, which produces a phospholipase D (PLD) with high transphosphatidylation activity. Here, we purified and cloned the PLD (PLD103) from the strain. PLD103 exerted the highest hydrolytic activity at a slightly alkaline pH, which is in contrast to the majority of known Streptomyces PLDs that have a slightly acidic optimum pH. PLD103 shares only 71-76% amino acid sequence identity with other Streptomyces PLDs that have a slightly acidic optimum pH; thus, the diversity in the primary structure might explain the discrepancy observed in the optimum pH. The purified PLD displayed high transphosphatidylation activity in the presence of glycerol, L: -serine, and 2-aminoethanol hydrochloride with a conversion rate of 82-97% in a simple one-phase system, which was comparable to the rate of other Streptomyces PLDs in a complicated biphasic system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1875-8355
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
598-608
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Purification, biochemical characterization, and cloning of phospholipase D from Streptomyces racemochromogenes strain 10-3.
pubmed:affiliation
Department of Food and Cosmetic Science, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri, Hokkaido 099-2493, Japan. y3nakaza@bioindustry.nodai.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't