Carbohydrate metabolism in Spirochaeta stenostrepta.
Journal: 1970/August - Journal of Bacteriology
ISSN: 0021-9193
PUBMED: 5423371
Abstract:
The pathways of carbohydrate metabolism in Spirochaeta stenostrepta, a free-living, strictly anaerobic spirochete, were studied. The organism fermented glucose to ethyl alcohol, acetate, lactate, CO(2), and H(2). Assays of enzymatic activities in cell extracts, and determinations of radioactivity distribution in products formed from (14)C-labeled glucose indicated that S. stenostrepta degraded glucose via the Embden-Meyerhof pathway. The spirochete utilized a clostridial-type clastic reaction to metabolize pyruvate to acetyl-coenzyme A, CO(2), and H(2), without production of formate. Acetyl-coenzyme A was converted to ethyl alcohol by nicotinamide adenine dinucleotide-dependent acetaldehyde and alcohol dehydrogenase activities. Phosphotransacetylase and acetate kinase catalyzed the formation of acetate from acetyl-coenzyme A. Hydrogenase and lactate dehydrogenase activities were detected in cell extracts. A rubredoxin was isolated from cell extracts of S. stenostrepta. Preparations of this rubredoxin stimulated acetyl phosphate formation from pyruvate by diethylaminoethyl cellulose-treated extracts of S. stenostrepta, an indication that rubredoxin may participate in pyruvate cleavage by this spirochete. Nutritional studies showed that S. stenostrepta fermented a variety of carbohydrates, but did not ferment amino acids or other organic acids. An unidentified growth factor present in yeast extract was required by the organism. Exogenous supplements of biotin, riboflavin, and vitamin B(12) were either stimulatory or required for growth.
Relations:
Content
Citations
(23)
References
(31)
Drugs
(4)
Chemicals
(14)
Organisms
(1)
Processes
(2)
Similar articles
Articles by the same authors
Discussion board
J Bacteriol 103(1): 216-226

Carbohydrate Metabolism in <em>Spirochaeta stenostrepta</em>

Abstract

The pathways of carbohydrate metabolism in Spirochaeta stenostrepta, a free-living, strictly anaerobic spirochete, were studied. The organism fermented glucose to ethyl alcohol, acetate, lactate, CO2, and H2. Assays of enzymatic activities in cell extracts, and determinations of radioactivity distribution in products formed from C-labeled glucose indicated that S. stenostrepta degraded glucose via the Embden-Meyerhof pathway. The spirochete utilized a clostridial-type clastic reaction to metabolize pyruvate to acetyl-coenzyme A, CO2, and H2, without production of formate. Acetyl-coenzyme A was converted to ethyl alcohol by nicotinamide adenine dinucleotide-dependent acetaldehyde and alcohol dehydrogenase activities. Phosphotransacetylase and acetate kinase catalyzed the formation of acetate from acetyl-coenzyme A. Hydrogenase and lactate dehydrogenase activities were detected in cell extracts. A rubredoxin was isolated from cell extracts of S. stenostrepta. Preparations of this rubredoxin stimulated acetyl phosphate formation from pyruvate by diethylaminoethyl cellulose-treated extracts of S. stenostrepta, an indication that rubredoxin may participate in pyruvate cleavage by this spirochete. Nutritional studies showed that S. stenostrepta fermented a variety of carbohydrates, but did not ferment amino acids or other organic acids. An unidentified growth factor present in yeast extract was required by the organism. Exogenous supplements of biotin, riboflavin, and vitamin B12 were either stimulatory or required for growth.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.5M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Bachmayer H, Piette LH, Yasunobu KT, Whiteley HR. The binding sites of iron in rubredoxin from Micrococcus aerogenes. Proc Natl Acad Sci U S A. 1967 Jan;57(1):122–127.[PMC free article] [PubMed] [Google Scholar]
  • Bachmayer H, Yasunobu KT, Peel JL, Mayhew S. Non-heme iron proteins. V. The amino acid sequence of rubredoxin from Peptostreptococcus elsdenii. J Biol Chem. 1968 Mar 10;243(5):1022–1030. [PubMed] [Google Scholar]
  • BARBAN S. Studies on the metabolism of the Treponemata. I. Amino acid metabolism. J Bacteriol. 1954 Oct;68(4):493–497.[PMC free article] [PubMed] [Google Scholar]
  • Breznak JA, Canale-Parola E. Spirochaeta aurantia, a pigmented, facultatively anaerobic spirochete. J Bacteriol. 1969 Jan;97(1):386–395.[PMC free article] [PubMed] [Google Scholar]
  • Canale-Parola E, Holt SC, Udris Z. Isolation of free-living, anaerobic spirochetes. Arch Mikrobiol. 1967;59(1):41–48. [PubMed] [Google Scholar]
  • Canale-Parola E, Udris Z, Mandel M. The classification of free-living spirochetes. Arch Mikrobiol. 1968;63(4):385–397. [PubMed] [Google Scholar]
  • DAWES EA, FOSTER SM. The formation of ethanol in Escherichia coli. Biochim Biophys Acta. 1956 Nov;22(2):253–265. [PubMed] [Google Scholar]
  • DOLIN MI, GUNSALUS IC. Pyruvic acid metabolism. II. An acetoinforming enzyme system in Streptococcus faecalis. J Bacteriol. 1951 Aug;62(2):199–214.[PMC free article] [PubMed] [Google Scholar]
  • FULTON JD, SMITH PJ. Carbohydrate metabolism in Spirochaeta recurrentis. 1. The metabolism of spirochaetes in vivo and in vitro. Biochem J. 1960 Sep;76:491–499.[PMC free article] [PubMed] [Google Scholar]
  • HAMILTON RD, WOLFE RS. Pyruvate exchange reactions in Bacillus macerans. J Bacteriol. 1959 Aug;78:253–258.[PMC free article] [PubMed] [Google Scholar]
  • Holt SC, Canale-Parola E. Fine structure of Spirochaeta stenostrepta, a free-living, anaerobic spirochete. J Bacteriol. 1968 Sep;96(3):822–835.[PMC free article] [PubMed] [Google Scholar]
  • Kupfer DG, Canale-Parola E. Pyruvate metabolism in Sarcina maxima. J Bacteriol. 1967 Oct;94(4):984–990.[PMC free article] [PubMed] [Google Scholar]
  • Lovenberg W, Sobel BE. Rubredoxin: a new electron transfer protein from Clostridium pasteurianum. Proc Natl Acad Sci U S A. 1965 Jul;54(1):193–199.[PMC free article] [PubMed] [Google Scholar]
  • LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  • McCormick NG, Ordal EJ, Whiteley HR. DEGRADATION OF PYRUVATE BY MICROCOCCUS LACTILYTICUS I. : General Properties of the Formate-Exchange Reaction. J Bacteriol. 1962 Apr;83(4):887–898.[PMC free article] [PubMed] [Google Scholar]
  • MORTLOCK RP, WOLFE RS. Reversal of pyruvate oxidation in Clostridium butyricum. J Biol Chem. 1959 Jul;234(7):1657–1658. [PubMed] [Google Scholar]
  • Newman DJ, Postgate JR. Rubredoxin from a nitrogen-fixing variety of Desulfovibrio desulfuricans. Eur J Biochem. 1968 Dec;7(1):45–50. [PubMed] [Google Scholar]
  • PECK HD, Jr, GEST H. A new procedure for assay of bacterial hydrogenases. J Bacteriol. 1956 Jan;71(1):70–80.[PMC free article] [PubMed] [Google Scholar]
  • PHARES EF. Degradation of labeled propionic and acetic acids. Arch Biochem Biophys. 1951 Sep;33(2):173–178. [PubMed] [Google Scholar]
  • ROSE IA, GRUNBERG-MANAGO M, KOREY SR, OCHOA S. Enzymatic phosphorylation of acetate. J Biol Chem. 1954 Dec;211(2):737–756. [PubMed] [Google Scholar]
  • Rudolph FB, Purich DL, Fromm HJ. Coenzyme A-linked aldehyde dehydrogenase from Escherichia coli. I. Partial purification, properties, and kinetic studies of the enzyme. J Biol Chem. 1968 Nov 10;243(21):5539–5545. [PubMed] [Google Scholar]
  • Sly LI, Doelle HW. Glucose-6-phosphate dehydrogenase in cell free extracts of Zymomonas mobilis. Arch Mikrobiol. 1968;63(3):197–213. [PubMed] [Google Scholar]
  • Sly LI, Doelle HW. 6-phosphogluconate dehydrogenase in cell free extracts of Escherichia coli K-12. Arch Mikrobiol. 1968;63(3):214–223. [PubMed] [Google Scholar]
  • Smith PJ. Carbohydrate metabolism in Spirochaeta recurrentis. 2. Enzymes associated with disintegrated cells and extracts of spirochaetes. Biochem J. 1960 Sep;76(3):500–508.[PMC free article] [PubMed] [Google Scholar]
  • STADTMAN ER, NOVELLI GD, LIPMANN F. Coenzyme A function in and acetyl transfer by the phosphotransacetylase system. J Biol Chem. 1951 Jul;191(1):365–376. [PubMed] [Google Scholar]
  • STRECKER HJ. Formate fixation in pyruvate by Escherichia coli. J Biol Chem. 1951 Apr;189(2):815–830. [PubMed] [Google Scholar]
  • Suh B, Akagi JM. Pyruvate-carbon dioxide exchange reaction of Desulfovibrio desulfuricans. J Bacteriol. 1966 Jun;91(6):2281–2285.[PMC free article] [PubMed] [Google Scholar]
  • VELDKAMP H. Isolation and characteristics of Treponema zuelzerae nov. spec., and anaerobic, free-living spirochete. Antonie Van Leeuwenhoek. 1960;26:103–125. [PubMed] [Google Scholar]
  • WHITELEY HR, McCORMICK NG. Degradation of pyruvate by Micrococcus lactilyticus. III. Properties and cofactor requirements of the carbon dioxide-exchange reaction. J Bacteriol. 1963 Feb;85:382–393.[PMC free article] [PubMed] [Google Scholar]
  • WOLFE RS, O'KANE DJ. Cofactors of the phosphoroclastic reaction of Clostridium butyricum. J Biol Chem. 1953 Dec;205(2):755–765. [PubMed] [Google Scholar]
  • WOLFE RS, O'KANE DJ. Cofactors of the carbon dioxide exchange reaction of Clostridium butyricum. J Biol Chem. 1955 Aug;215(2):637–643. [PubMed] [Google Scholar]
Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01002
Abstract
The pathways of carbohydrate metabolism in Spirochaeta stenostrepta, a free-living, strictly anaerobic spirochete, were studied. The organism fermented glucose to ethyl alcohol, acetate, lactate, CO2, and H2. Assays of enzymatic activities in cell extracts, and determinations of radioactivity distribution in products formed from C-labeled glucose indicated that S. stenostrepta degraded glucose via the Embden-Meyerhof pathway. The spirochete utilized a clostridial-type clastic reaction to metabolize pyruvate to acetyl-coenzyme A, CO2, and H2, without production of formate. Acetyl-coenzyme A was converted to ethyl alcohol by nicotinamide adenine dinucleotide-dependent acetaldehyde and alcohol dehydrogenase activities. Phosphotransacetylase and acetate kinase catalyzed the formation of acetate from acetyl-coenzyme A. Hydrogenase and lactate dehydrogenase activities were detected in cell extracts. A rubredoxin was isolated from cell extracts of S. stenostrepta. Preparations of this rubredoxin stimulated acetyl phosphate formation from pyruvate by diethylaminoethyl cellulose-treated extracts of S. stenostrepta, an indication that rubredoxin may participate in pyruvate cleavage by this spirochete. Nutritional studies showed that S. stenostrepta fermented a variety of carbohydrates, but did not ferment amino acids or other organic acids. An unidentified growth factor present in yeast extract was required by the organism. Exogenous supplements of biotin, riboflavin, and vitamin B12 were either stimulatory or required for growth.
Collaboration tool especially designed for Life Science professionals.Drag-and-drop any entity to your messages.