Shinohe_1996_FEMS.Microbiol.Lett_141_103

Reference

Title : Determination of the active sites serine of the poly (3-hydroxybutyrate) depolymerases of Pseudomonas lemoignei (PhaZ5) and of Alcaligenes faecalis - Shinohe_1996_FEMS.Microbiol.Lett_141_103
Author(s) : Shinohe T , Nojiri M , Saito T , Stanislawski T , Jendrossek D
Ref : FEMS Microbiology Letters , 141 :103 , 1996
Abstract :

Mutational analysis of the poly(3-hydroxybutyrate) (PHB) depolymerase A of Pseudomonas lemoignei and of the poly(3-hydroxybutyrate) depolymerase of Alcaligenes faecalis revealed that S138 (P. lemoignei) and S139 (A. faecalis) are essential for activity. Both serines are part of a strictly conserved pentapeptide sequence which is present in all poly(3-hydroxybutyrate) depolymerases analyzed so far (G-L-S-S(A)-G) and which resembles the lipase box of lipases and other serine hydrolases (G-X-S-X-G). Mutation of another conserved serine, namely S195 (P. lemoignei) and S196 (A. faecalis), resulted in mutant proteins with almost full activity and proved that S195 and S196 are not essential for activity. The results indicate the structural and functional relationship of poly(3-hydroxybutyrate) depolymerases to the family of serine hydrolases.

PubMedSearch : Shinohe_1996_FEMS.Microbiol.Lett_141_103
PubMedID: 8764515

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Citations formats

Shinohe T, Nojiri M, Saito T, Stanislawski T, Jendrossek D (1996)
Determination of the active sites serine of the poly (3-hydroxybutyrate) depolymerases of Pseudomonas lemoignei (PhaZ5) and of Alcaligenes faecalis
FEMS Microbiology Letters 141 :103

Shinohe T, Nojiri M, Saito T, Stanislawski T, Jendrossek D (1996)
FEMS Microbiology Letters 141 :103