Purification and characterization of an erythromycin esterase from an erythromycin-resistant Pseudomonas sp

An erythromycin esterase (molecular mass 51 200 Da) was purified from Pseudomonas sp. GD100, which was isolated from a salmon hatchery sediment sample from Washington State. The p I of the protein was 4.5–4.8. The enzyme was inhibited by 1 mM mercuric acid, and had the substrate specificity for stru...

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Bibliographic Details
Published inFEMS microbiology letters Vol. 210; no. 2; pp. 239 - 244
Main Authors Kim, Yong-Hak, Cha, Chang-Jun, Cerniglia, Carl E.
Format Journal Article
LanguageEnglish
Published Elsevier B.V 07.05.2002
Subjects
Aquaculture
Erythromycin A
Erythromycin A enol ether
Mercuric chloride
Oleandomycin
Erythromycin A
Erythromycin A enol ether
Oleandomycin
Mercuric chloride
Aquaculture
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Summary:An erythromycin esterase (molecular mass 51 200 Da) was purified from Pseudomonas sp. GD100, which was isolated from a salmon hatchery sediment sample from Washington State. The p I of the protein was 4.5–4.8. The enzyme was inhibited by 1 mM mercuric acid, and had the substrate specificity for structurally related 14-membered macrolides, which decreased in the order of oleandomycin, erythromycin A and erythromycin A enol ether. The activity for erythromycin A varied with temperature, but the effect of pH was minimal at pH 6.0–9.0. The half-life of the enzyme was estimated to be 8.9 h at 35°C and 0.23 h at 55°C, and the activation energy of the catalytic reaction of erythromycin A was estimated at 16.2 kJ mol −1.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(02)00611-0