Formation of adenosine 5'-tetraphosphate from the acyl phosphate intermediate: a difference between the MurC and MurD synthetases of Escherichia coli.
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.
Biochimie Structurale et Cellulaire, EP 1088 CNRS, Université de Paris-Sud, Orsay, France.
A
A
Bouhss
S
S
Dementin
J
J
van Heijenoort
C
C
Parquet
D
D
Blanot
D000215:Acylation; D000227:Adenine Nucleotides / Q000096:biosynthesis*; D010755:Organophosphates / Q000378:metabolism; D010453:Peptide Synthases / Q000737:chemistry / Q000378:metabolism*
D000227:Adenine Nucleotides; D010755:Organophosphates; C017991:adenosine 5'-tetraphosphate; D010453:Peptide Synthases; C023229:UDP-N-acetylmuramoyl-alanine synthetase; C053379:UDP-N-acetylmuramoylalanine-D-glutamate ligase