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At least 343 records · Page 19Linked to original sources
PubMed1969

Assay and properties of diaminopimelate epimerase from Bacillus megaterium.

1. Diaminopimelate epimerase from a soluble extract of Bacillus megaterium N.C.I.B. 7581 was purified about 25-fold by fractionation with ammonium sulphate and chromatography on calcium phosphate gel-cellulose. The product was impure but was unstable on further purification. 2. Quantitative assay methods for the enzyme were devised in which meso- or ll-diaminopimelic acid may be the substrate. 3. Between 25 degrees and 45 degrees at pH7.0 enzyme action leads to an equilibrium mixture containing 65% meso-isomer and 35% ll-isomer. 4. The initial rate of epimerization was 2-3 times as fast with ll-diaminopimelic acid as substrate as with the meso-isomer; a number of other amino acids were not racemized by the enzyme. The Michaelis constants at 37 degrees were 6.7mm (ll-isomer) and 100mm (meso-isomer); with both substrates enzyme activity was maximal at pH7-8. The relative rates of epimerization of ll-diaminopimelic acid at 25 degrees , 37 degrees and 45 degrees were 0.77:1.00:1.15. 5. A thiol compound (of which 2,3-dimercaptopropan-1-ol was the most effective) was needed as an activator of the purified enzyme. 6. Carbonylbinding reagents and several other compounds did not inhibit diaminopimelate epimerase. 7. Pyridoxal phosphate did not stimulate enzymic activity even in preparations that had been almost completely freed of derivatives of vitamin B(6) (as shown by microbiological assay).

Amino Acids↗
PubMed1972

Studies on Escherichia coli enzymes involved in the synthesis of uridine diphosphate-N-acetyl-muramyl-pentapeptide.

The specific activities of l-alanine:d-alanine racemase, d-alanine:d-alanine ligase, and the l-alanine, d-glutamic acid, meso-diaminopimelic acid, and d-alanyl-d-alanine adding enzymes were followed during growth of Escherichia coli. The specific activities were nearly independent of the growth phase. d-Alanine:d-alanine ligase was inhibited by d-alanyl-d-alanine, d-cycloserine, glycine, and glycyl-glycine. l-Alanine:d-alanine racemase was found to be sensitive to d-cycloserine, glycine, and glycyl-glycine. The l-alanine adding enzyme was inhibited by glycine and glycyl-glycine.

Acetates↗
PubMed1968

The cell wall of Bacillus licheniformis N.C.T.C. 6346. Composition of the mucopeptide component.

1. The mucopeptide component of wall preparations from Bacillus licheniformis was obtained in soluble form by treatment of the acid-insoluble residue of walls with lysozyme. 2. The soluble mucopeptide contains glutamic acid, diaminopimelic acid, alanine, N-acetylglucosamine and N-acetylmuramic acid in the molecular proportions 1.0:1.0:1.6:0.8:0.7. In addition approx. 1 mole of amide/mole of glutamic acid is present. Essentially all of the dry weight and nitrogen content of soluble mucopeptide is accounted for by these constituents. 3. The optical configurations of the amino acids were determined. Approx. 0.6 mole of d-alanine and 1.0 mole of l-alanine are present/mole of glutamic acid. 4. The structures of several small peptides derived from soluble mucopeptide after mild acid hydrolysis were established. 5. The structure of soluble mucopeptide from B. licheniformis is discussed on the basis of these results together with data on the number of free amino groups present in soluble mucopeptide.

Alanine↗
PubMed1974

Threonine locus of Escherichia coli K-12: genetic structure and evidence for an operon.

Three genes, thrA, thrB, and thrC, were previously defined and localized in the threonine locus of Escherichia coli K-12. thrA, thrB, and thrC specify the enzymes aspartokinase I-homoserine dehydrogenase I, homoserine kinase, and threonine synthetase, respectively. A complementation analysis of the threonine cluster using derivatives of a lambda phage carrying the threonine genes (lambdadthr(c)) demonstrates that: (i) thrB and thrC each consist of a single cistron; and (ii) thrA is composed of two cistrons, thrA(1) and thrA(2), although it specifies a single polypeptide chain. thrA(1) and thrA(2) correspond to aspartokinase I and homoserine dehydrogenase I, respectively. Their relative order is established. The demonstration of polar effects of mutations (nonsense or induced by phage Mu) in thrA and thrB is taken as evidence for the existence of a thrA thrB thrC operon, transcribed in this order.

Alcohol Oxidoreductases↗
PubMed1998

Biochemical and genetic characterization of a gentisate 1, 2-dioxygenase from Sphingomonas sp. strain RW5.

A 4,103-bp long DNA fragment containing the structural gene of a gentisate 1,2-dioxygenase (EC 1.13.11.4), gtdA, from Sphingomonas sp. strain RW5 was cloned and sequenced. The gtdA gene encodes a 350-amino-acid polypeptide with a predicted size of 38.85 kDa. Comparison of the gtdA gene product with protein sequences in databases, including those of intradiol or extradiol ring-cleaving dioxygenases, revealed no significant homology except for a low similarity (27%) to the 1-hydroxy-2-naphthoate dioxygenase (phdI) of the phenanthrene degradation in Nocardioides sp. strain KP7 (T. Iwabuchi and S. Harayama, J. Bacteriol. 179:6488-6494, 1997). This gentisate 1,2-dioxygenase is thus a member of a new class of ring-cleaving dioxygenases. The gene was subcloned and hyperexpressed in E. coli. The resulting product was purified to homogeneity and partially characterized. Under denaturing conditions, the polypeptide exhibited an approximate size of 38.5 kDa and migrated on gel filtration as a species with a molecular mass of 177 kDa. The enzyme thus appears to be a homotetrameric protein. The purified enzyme stoichiometrically converted gentisate to maleylpyruvate, which was identified by gas chromatography-mass spectrometry analysis as its methyl ester. Values of affinity constants (Km) and specificity constants (Kcat/Km) of the enzyme were determined to be 15 microM and 511 s-1 M-1 x 10(4) for gentisate and 754 microM and 20 s-1 M-1 x 10(4) for 3, 6-dichlorogentisate. Three further open reading frames (ORFs) were found downstream of gtdA. The deduced amino acid sequence of ORF 2 showed homology to several isomerases and carboxylases, and those of ORFs 3 and 4 exhibited significant homology to enzymes of the glutathione isomerase superfamily and glutathione reductase superfamily, respectively.

Amino Acid Sequence↗
PubMed1968

Peptidoglycan of a chemolithotrophic bacterium, Ferrobacillus ferrooxidans.

The rigid layer (peptidoglycan) of the wall of the chemolithotroph Ferrobacillus ferrooxidans was isolated after various chemical treatments. The removal of specific components was followed by noting in an electron microscope changes in the appearance of the cell surface. The final peptidoglycan was virtually free from proteins and was sensitive to the action of lysozyme. Results of chemical analyses of acidhydrolyzed peptidoglycan revealed three major amino acids and two amino sugars: glutamic acid, alpha,epsilon-diaminopimelic acid, alanine, glucosamine, and muramic acid in a ratio of 1:1:2.33:062:088.

Alanine↗
PubMed1972

Bacteriolytic enzymes produced by Myxococcus xanthus.

The bacteriolytic activities in the culture fluid of Myxococcus xanthus were purified and separated into six active fractions by the use of Bio-Gel CM-2 and Bio-Gel P-60. These fractions were identified as: (i) an amidase, (ii) a glucosaminidase, (iii) a glucosaminidase and an amidase, (iv) a protease with probable amidase activity, (v) another protease with probable amidase activity, and (vi) a peptidase active on both d-alanyl-diaminopimelate and d-alanyl-lysine peptide bonds. On one occasion, another amidase was eluted from Bio-Gel CM. Preliminary studies on some characteristics of the enzymes and their production during growth are reported.

Alanine↗
PubMed1975

Control of lysine biosynthesis in Bacillus subtilis: inhibition of diaminopimelate decarboxylase by lysine.

Diaminopimelate decarboxylase has been characterized in extracts of Bacillus subtilis and resolved from aspartokinases I and II. Under certain conditions, the enzyme is specifically inhibited by physiological concentrations of L-lysine, but less specificity and altered kinetics of inhibition are observed if lower ionic strengths are employed in the assay procedure. Diaminopimelate decarboxylase can be desensitized to lysine inhibition by either lowering the pH or diluting the enzyme in Tris buffer in the absence of pyridoxal phosphate. Evidence is presented to incidate that, under proper conditions, lysine inhibition involves an interaction of the amino acid with the enzyme rather than competition for available pyridoxal phosphate in the assay. Lysine, by affecting the level of meso-diaminopimelate, may thus regulate its biosynthesis through sequential feedback inhibition. Analysis of the diaminopimelate decarboxylase of 15 revertants of mutants that had originally lacked diaminopimelate decarboxylase activity indicates that as little as 5% of the specific activity of enzyme observed in the wild-type strain is sufficient to permit normal growth rates. In the growing cell, diaminopimelate decarboxylase may therefore exist largely in an inhibited state.

Aspartic Acid↗
PubMed1973

Aspartokinase activity and the developmental cycle of Myxococcus xanthus.

The relationship between aspartokinase activity and fruiting body formation in Myxococcus xanthus was investigated. Two required amino acids, methionine and isoleucine, which stimulated the enzyme in vitro also inhibited fruiting body formation when added to 0.1% Casitone agar. Threonine, a potent feedback inhibitor of the aspartokinase, completely reversed the effects of methionine and isoleucine both on enzyme activity and fruiting body formation. A mutant, M. xanthus FB-S, which had the unusual property of forming fruiting bodies on 1.0% Casitone agar, also exhibited an altered regulation of aspartokinase activity. Spermidine, which is a strong stimulator of the enzyme in vitro, interfered with the developmental cycle of both M. xanthus FB and FS-S. During glycerol induction of myxospores the level of aspartokinase dropped more than 75% during the first hour. These data indicate a strong correlation between aspartokinase activity and the induction of the developmental cycle in M. xanthus. It is suggested that the decrease in aspartokinase activity results in diaminopimelic acid starvation, blockage of cell wall growth, and subsequent induction of the developmental cycle.

Agar↗