Abstract
Moore, L. Daneo (University of Pennsylvania, Philadelphia) and D. J. O'Kane. Kinases of Streptococcus faecalis. I. Enzyme localization. J. Bacteriol. 86:766–772. 1963.—Cell-free extracts of Streptococcus faecalis 10C1 were found to contain a membrane-associated, particulate hexokinase with activity toward glucose, fructose, mannose, and, to a lesser extent, galactose, gluconate, and mannitol. In addition, the cell cytoplasm contained kinases specific for fructose, mannose, and galactose. No specific kinases were found for gluconate or mannitol, although in the presence of mannitol adenosine triphosphate was utilized by a cytoplasmic fraction. The possibility is discussed that the main pathways of gluconate and mannitol metabolism are oxidation followed by phosphorylation.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ALEXANDER M. Localization of enzymes in the microbial cell. Bacteriol Rev. 1956 Jun;20(2):67–93. doi: 10.1128/br.20.2.67-93.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BEST J. B. The inference of intracellular enzymatic properties from kinetic data obtained on living cells. II. A study of hexokinase and invertase as cellular components of baker's yeast. J Cell Physiol. 1955 Aug;46(1):29–52. doi: 10.1002/jcp.1030460103. [DOI] [PubMed] [Google Scholar]
- COTA-ROBLES E. H., MARR A. G., NILSON E. H. Submicroscopic particles in extracts of Azotobacter agilis. J Bacteriol. 1958 Mar;75(3):243–252. doi: 10.1128/jb.75.3.243-252.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DE LEY J., VANDAMME J. The metabolism of sodium 2-keto-D-gluconate by micro-organisms. J Gen Microbiol. 1955 Apr;12(2):162–171. doi: 10.1099/00221287-12-2-162. [DOI] [PubMed] [Google Scholar]
- GAMMACK D. B., HUEHNS E. R., SHOOTER E. M., GERALD P. S. Identification of the abnormal polypeptide chain of hemoglobin G-Ib. J Mol Biol. 1960 Dec;2:372–378. doi: 10.1016/s0022-2836(60)80048-4. [DOI] [PubMed] [Google Scholar]
- LANGE C. F., Jr, KOHN P. Substrate specificity of hexokinases. J Biol Chem. 1961 Jan;236:1–5. [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- MARKERT C. L., APPELLA E. Physicochemical nature of isozvmes. Ann N Y Acad Sci. 1961 Nov 2;94:678–690. doi: 10.1111/j.1749-6632.1961.tb35565.x. [DOI] [PubMed] [Google Scholar]
- MARR A. G., COTA-ROBLES E. H. Sonic disruption of Azotobacter vinelandil. J Bacteriol. 1957 Jul;74(1):79–86. doi: 10.1128/jb.74.1.79-86.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MATHEWS M. M., SISTROM W. R. Intracellular location of carotenoid pigments and some respiratory enzymes in Sarcina lutea. J Bacteriol. 1959 Dec;78:778–787. doi: 10.1128/jb.78.6.778-787.1959. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NEWTON J. W., NEWTON G. A. Composition of the photoactive subcellular particles from Chromatium. Arch Biochem Biophys. 1957 Sep;71(1):250–265. doi: 10.1016/0003-9861(57)90026-7. [DOI] [PubMed] [Google Scholar]
- SMITHIES O. Zone electrophoresis in starch gels and its application to studies of serum proteins. Adv Protein Chem. 1959;14:65–113. doi: 10.1016/s0065-3233(08)60609-9. [DOI] [PubMed] [Google Scholar]
- SOKATCH J. T., GUNSALUS I. C. Aldonic acid metabolism. I. Pathway of carbon in an inducible gluconate fermentation by Streptococcus faecalis. J Bacteriol. 1957 Apr;73(4):452–460. doi: 10.1128/jb.73.4.452-460.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SOLS A., CRANE R. K. Substrate specificity of brain hexokinase. J Biol Chem. 1954 Oct;210(2):581–595. [PubMed] [Google Scholar]
- SOLS A., DE LA FUENTE G., VILLARPALASI C., ASENSIO C. Substrate specificity and some other properties of baker's yeast hexokinase. Biochim Biophys Acta. 1958 Oct;30(1):92–101. doi: 10.1016/0006-3002(58)90245-2. [DOI] [PubMed] [Google Scholar]