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PubMed1976

Synthesis of the monomer and dimer peptide fragments of the Micrococcus lysodeikticus cell wall peptidoglycan.

Three branched peptides, namely pentapeptide A and the two decapeptides B and C corresponding respectively to the monomer and the two dimer peptide fragments of the M. lysodeikticus cell wall peptidoglycan, were synthetized by adequate methods of peptide synthesis in homogeneous phase. The synthetized peptides showed the same electrophoretic and chromatographic behavior as the natural peptide fragments. Only decapeptide B was hydrolysed by the Myxobacter AL-1 protease by cleavage of the D-Ala-L-Ala bond and inversely, only decapeptide C was digested by the Streptomyces albus ML endopeptidase by cleavage of the D-Ala-epsilon-Lys linkage. In both enzymatic hydrolyses the pentapeptide monomer was formed.

Amino Acids↗
PubMed1981

Stereochemical and kinetic investigation of 32P-labeled inorganic phosphate exchange reaction catalyzed by primer-independent and primer-dependent polynucleotide phosphorylase from Micrococcus luteus.

The SP diastereomer of adenosine 5'-O-(1-thiodiphosphate) (ADP alpha S) is a substrate for the 32P-labeled inorganic phosphate exchange reaction catalyzed by the T and I forms of polynucleotide phosphorylase. The exchange reaction occurs with retention of configuration. This exchange reaction is very slow when only ADP alpha S(SP) is presented but is greatly activated by dinucleotide primers and ADP alpha S(RP), although the latter is not a substrate for the exchange reaction. Ap(S)A(RP) is an approximately 50% better activator of the exchange than the SP diastereomer. Furthermore, high levels of the ADP alpha S(SP) eliminate the activation by primers and by ADP alpha S(RP). A phosphatase activity is present with the I form of the enzyme which converts ADP alpha S(RP) to AMPS. This activity may be responsible for the formation of the 5'-phosphate end group for de novo polymerization or for the processivity of this reaction.

Adenosine Diphosphate↗
PubMed1979

Stereochemistry of internucleotide bond formation by polynucleotide phosphorylase from Micrococcus luteus.

Polynucleotide phosphorylase catalyzes the formation of polynucleotides from the Sp diastereomer of adenosine 5'-O-(l-thiodiphosphate) ADPalphaS), whereas the Rp diastereomer is a competitive inhibitor. The absolute configuration of the phosphorothioate diester bond in the polymer was determined by copolymerizing ADPalpha S, Sp isomer with UDP and degrading the resulting copolymer with R Nase A and spleen phosphodiesterase to give, inter alia, uridine 2',-3'-cyclic phosphorothioate. The latter product was shown to be the endo isomer by high-performance liquid chromatography. No evidence for the presence of the exo isomer was obtained. It can thus be concluded that the Sp diastereomer of ADPalphaS polymerizes with inversion of configuration at phosphorus without racemization to give a phosphorothioate diester bond with the Rp configuration.

Kinetics↗