| Autor: |
Zorn, Holger, Bouws, Henning, Takenberg, Meike, Nimtz, Manfred, Getzlaff, Rita, Breithaupt, Dietmar E., Berger, Ralf G. |
| Předmět: |
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| Zdroj: |
Biological Chemistry; May2005, Vol. 386 Issue 5, p435-440, 6p, 3 Diagrams, 1 Chart, 3 Graphs |
| Abstrakt: |
An extracellular enzyme capable of efficient hydrolysis of xanthophyll esters was purified from culture supernatants of the basidiomycete Pleurotus sapidus . Under native conditions, the enzyme exhibited a molecular mass of 430 kDa, and SDS-PAGE data suggested a composition of eight identical subunits. Biochemical characterisation of the purified protein showed an isoelectric point of 4.5, and ideal hydrolysis conditions were observed at pH 5.8 and 40°C. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. An 1861-bp cDNA containing an open reading frame of 1641 bp was cloned from a cDNA library that showed ca. 40% homology to Candida rugosa lipases. The P. sapidus carboxylesterase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus that has been characterised at the molecular level. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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