ArticleThe protein journal2010
Purification, biochemical characterization, and cloning of phospholipase D from Streptomyces racemochromogenes strain 10-3.
Article in The protein journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 17 citations in OpenAlex.
- Development of a thiostrepton-free system for stable production of PLD in Streptomyces lividans SBT5.Microbial cell factories · 2022Article
- ARTP mutagenesis of phospholipase D-producing strainHeliyon · 2022Article
- Calcium-Induced Lipid Nanocluster Structures: Sculpturing of the Plasma Membrane.Biochemistry · 2018Article
- Molecular cloning, heterologous expression, and enzymatic characterization of lysoplasmalogen-specific phospholipase D fromFEBS open bio · 2016Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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