Biosynthesis of D-alanyl-lipoteichoic acid by Lactobacillus casei: interchain transacylation of D-alanyl ester residues
Lipoteichoic acid (LTA) from Lactobacillus casei contains poly(glycerophosphate) substituted with D-alanyl ester residues. The distribution of these residues in the in vitro-synthesized polymer is uniform. Esterification of LTA with D-alanine may occur in one of two modes: (i) addition at random or (ii) addition at a defined locus in the poly(glycerophosphate) chain followed by redistribution of the ester residues. A time-dependent transacylation of these residues from D-(/sup 14/C)alanyl-lipophilic LTA to hydrophilic acceptor was observed. The hydrophilic acceptor was characterized as D-alanyl-hydrophilic LTA. This transacylation requires neither ATP nor the D-alanine incorporation system, i.e., the D-alanine activating enzyme and D-alanine:membrane acceptor ligase. No evidence for an enzyme-catalyzed transacylation reaction was observed. The authors propose that this process of transacylation may be responsible for the redistribution of D-alanyl residues after esterification to the poly(glycerophosphate). As a result, it is difficult to distinguish between these proposed modes of addition.
- OSTI ID:
- 6432568
- Journal Information:
- J. Bacteriol.; (United States), Vol. 3
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ORGANIC ACIDS
ESTERIFICATION
RESIDUES
ACYLATION
ATP
CARBON 14 COMPOUNDS
ESTERS
LACTOBACILLUS
LIGASES
PHOSPHATES
TIME DEPENDENCE
TRACER TECHNIQUES
BACTERIA
CHEMICAL REACTIONS
ENZYMES
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MICROORGANISMS
NUCLEOTIDES
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PHOSPHORUS COMPOUNDS
550201* - Biochemistry- Tracer Techniques