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Title: Riboflavin production during growth of Micrococcus luteus on pyridine

Abstract

Micrococcus luteus produced 29 {mu}M riboflavin during growth on 6.5 mM pyridine but not during growth on other substrates. On the basic of the results of radiolabelling studies, riboflavin was not directly synthesized from pyridine. Pyridine may interfere with riboflavin biosynthesis or elicit a general stress response in M. luteus. The optimum concentration of pyridine for both growth of the organism and pyridine degradation was 13 mM. Above 25 mM, pyridine temporarily inhibited growth, pyridine degradation, oxygen uptake, and pigment production.

Authors:
 [1];  [2]
  1. (Environmental Chemistry Lab., Dow Elanco, Midland, MI (United States))
  2. (Ohio State Univ., Columbus (United States))
Publication Date:
OSTI Identifier:
6952148
Resource Type:
Journal Article
Resource Relation:
Journal Name: Applied and Environmental Microbiology; (United States); Journal Volume: 58:10
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; 54 ENVIRONMENTAL SCIENCES; MICROCOCCUS; METABOLISM; PYRIDINES; RIBOFLAVIN; BIOSYNTHESIS; BIOLOGICAL STRESS; GROWTH; TOXICITY; AZINES; BACTERIA; HETEROCYCLIC COMPOUNDS; MICROORGANISMS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; SYNTHESIS; VITAMIN B GROUP; VITAMINS 560300* -- Chemicals Metabolism & Toxicology; 540210 -- Environment, Terrestrial-- Basic Studies-- (1990-)

Citation Formats

Sims, G.K., and O'Loughlin, E.J.. Riboflavin production during growth of Micrococcus luteus on pyridine. United States: N. p., 1992. Web.
Sims, G.K., & O'Loughlin, E.J.. Riboflavin production during growth of Micrococcus luteus on pyridine. United States.
Sims, G.K., and O'Loughlin, E.J.. 1992. "Riboflavin production during growth of Micrococcus luteus on pyridine". United States. doi:.
@article{osti_6952148,
title = {Riboflavin production during growth of Micrococcus luteus on pyridine},
author = {Sims, G.K. and O'Loughlin, E.J.},
abstractNote = {Micrococcus luteus produced 29 {mu}M riboflavin during growth on 6.5 mM pyridine but not during growth on other substrates. On the basic of the results of radiolabelling studies, riboflavin was not directly synthesized from pyridine. Pyridine may interfere with riboflavin biosynthesis or elicit a general stress response in M. luteus. The optimum concentration of pyridine for both growth of the organism and pyridine degradation was 13 mM. Above 25 mM, pyridine temporarily inhibited growth, pyridine degradation, oxygen uptake, and pigment production.},
doi = {},
journal = {Applied and Environmental Microbiology; (United States)},
number = ,
volume = 58:10,
place = {United States},
year = 1992,
month =
}
  • An organism capable of growth on pyridine was isolated from soil by enrichment culture techniques and identified as Micrococcus luteus. The organism oxidized pyridine for energy and released N contained in the pyridine ring as ammonium. The organism could not grow on mono- or disubstituted pyridinecarboxylic acids or hydroxy-, chloro-, amino-, or methylpyridines. Cell extracts of M. luteus could not degrade pyridine, 2-, 3-, or 4-hydroxypyridines or 2,3-dihydroxypyridine, regardless of added cofactors or cell particulate fraction. The organism had a NAD-linked succinate-semialdehyde dehydrogenase which was induced by pyridine. Cell extracts of M. luteus had constitutive amidase activity, and washed cellsmore » degraded formate and formamide without a lag. These data are consistent with a previously reported pathway for pyridine metabolism by species of Bacillus, Brevibacterium, and Corynebacterium. Cells of M. luteus were permeable to pyridinecarboxylic acids, monohydroxypyridines, 2,3-dihydroxypyridine, and monoamino- and methylpyridines. The results provide new evidence that the metabolism of pyridine by microorganisms does not require initial hydroxylation of the ring and that permeability barriers do not account for the extremely limited range of substrate isomers used by pyridine degraders.« less
  • Py--Py correndonucleases I and II from Micrococcus luteus act exclusively on thymine-thymine, cytosine-cytosine, and thymine-cytosine cyclobutyl dimers in DNA, catalyzing incision 5' to the damage and generating 3'-hydroxyl and 5'-phosphoryl termini. Both enzymes initiate excision of pyrimidine dimers in vitro by correxonucleases and DNA polymerase I. The respective incised DNAs, however, differ in their ability to act as substrate for phage T4 polynucleotide ligase or bacterial alkaline phosphatase, suggesting that each endonuclease is specific for a conformationally unique site. The possibility that their respective action generates termini which represent different degrees of single strandedness is suggested by the unequal protectionmore » by Escherichia coli binding protein from the hydrolytic action of exonuclease VII.« less
  • Involvement of Py--Py correndonucleases I and II in repair of ultraviolet radiation damage in vivo by Micrococcus luteus has been demonstrated by their absence in the ultraviolet-sensitive mutant DB-7 derived by treatment of the wild type parent with N-methyl-N'-nitro-N-nitrosoguanidine. The necessity for their combined action in DNA repair in M. luteus is shown by: (a) reactivation of ultraviolet-damaged phiX174 RFI DNA in incision-defective hosts after in vivo treatment with both enzymes, (b) correlation between survival after ultraviolet irradiation and the level of the two enzymes, and (c) increased levels of repair synthesis after ultraviolet irradiation of toluenized cells DB-400 withmore » wild type correndonuclease levels when compared with the transformant DB-200 and the mutant DB-7, which lack one or both enzymes.« less
  • Five peaks of endonuclease activity showing a preference for ultraviolet-damaged DNA have been chromatographically identified from extracts of Micrococcus luteus. They are numerically designated as I to V in order of their elution from phosphocellulose (Whatman P-11) columns. The first two of these peaks have been highly purified by a combination of gel filtration and affinity chromatography and are catalytically homogeneous judging from their effect on transforming DNAs. Peak I, which has an isoelectric point of 4.7, is heat-stable, requires high ionic strength for optimal activity, acts with equal facility on ultraviolet-irradiated native and denatured DNA, and has been designatedmore » as Py--Py correndonuclease I. Peak II which has a pI value of 8.7, is heat-labile, is inhibited by high ionic strength, acts on ultraviolet-irradiated native but not denatured DNA, and has been designated as Py--Py correndonuclease II. Both enzymes are inhibited by Ca/sup 2 +/ and Zn/sup 2 +/, do not show any cofactor or sulfhydryl requirement, act optimally between pH 7.0 and 7.4, and have molecular weights between 11,000 and 15,000. Py--Py correndonuclease I requires a dose about 1.6 times that for Py--Py correndonuclease II for incision saturation of irradiated phiX174 RFI DNA.« less