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Formation of adenosine 5′‐tetraphosphate from the acyl phosphate intermediate: a difference between the MurC and MurD synthetases of Escherichia coli
Author(s) -
Bouhss Ahmed,
Dementin Sébastien,
van Heijenoort Jean,
Parquet Claudine,
Blanot Didier
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00684-5
Subject(s) - chemistry , escherichia coli , adenosine , phosphate , adenosine triphosphate , biochemistry , stereochemistry , gene
The mechanism of the Mur synthetases of peptidoglycan biosynthesis is thought to involve in each case the successive formation of an acyl phosphate and a tetrahedral intermediate. The existence of the acyl phosphates for the MurC and MurD enzymes from Escherichia coli was firmly established by their in situ reduction by sodium borohydride followed by acid hydrolysis, yielding the corresponding amino alcohols. Furthermore, it was found that MurD, but not MurC, catalyses the synthesis of adenosine 5′‐tetraphosphate from the acyl phosphate, thereby substantiating its existence and pointing out a difference between the two enzymes.