Characterization of two N-acetyl muramoylhydrolases of Streptococcus faecium ATCC 9790

Thesis/Dissertation · Fri Jan 01 00:00:00 EST 1988

OSTI ID:5649272

Dolinger, D L

Purified muramidase-1 of S. faecium has been shown to contain a covalently attached nucleotide. The nucleotide was isolated and identified as 5-mercaptouridine monophosphate, and to occur as multiple monomeric substitutions on the polypeptide chain, via a phosphodiester bond. Exhaustive proteolytic hydrolysis of purified muramidase-1 yielded a peptide fragment consisting of 5-mercaptouridine, tyrosine, alanine, glycine, and leucine. A second peptidoglycan hydrolase (muramidase-2) has been purified to apparent homogeneity. The enzymatic activity has been shown to be consistent with that of a 3-1,4-N-acetylmuramoylhydrolase and differs in substrate specificity and possibility mechanism of hydrolysis from muramidase-1. Purified enzyme appears as two protein staining bands of molecular masses 125 and 75 kDa after sodium dodecylsulfate polyacrylamide gel ectrophoresis. Elution and renaturation of the protein bands showed that both proteins contain muramidase-2 activity. In addition both proteins have also been shown to specifically bind ({sup 14}C)penicillin G and been tentatively identified as penicillin binding proteins 1 and 5, respectively.

• Research Organization: Temple Univ., Philadelphia, PA (USA)
• OSTI ID: 5649272
• Resource Relation: Other Information: Thesis (Ph. D.)
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
HYDROLASES
CHEMICAL COMPOSITION
BIOCHEMICAL REACTION KINETICS
CARBON 14 COMPOUNDS
ELECTROPHORESIS
ENZYME ACTIVITY
FRACTIONATION
HYDROLYSIS
NUCLEOTIDES
PENICILLIN
STREPTOCOCCUS
TRACER TECHNIQUES
ANTI-INFECTIVE AGENTS
ANTIBIOTICS
BACTERIA
CHEMICAL REACTIONS
DECOMPOSITION
DRUGS
ENZYMES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
LYSIS
MICROORGANISMS
ORGANIC COMPOUNDS
REACTION KINETICS
SEPARATION PROCESSES
SOLVOLYSIS
550201* - Biochemistry- Tracer Techniques