Chapter 10 A life-long quest for biochemical regulation (Helmut Holzer, 1921-1997)

Comprehensive Biochemistry

Volumn 41, Issue C, 2000, Pages 531-561

  Decker, Karl ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

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[No Author keywords available]

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EID: 25844464101     PISSN: 00698032     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0069-8032(00)41014-4     Document Type: Article

References (56)

1. Holzer H., and Lynen F. Über den aeroben Phosphatbedarf der Hefe III. Liebigs Ann. Chem. 569 (1950) 138-148
2. Lipmann F. A phosphorylated oxidation product of pyruvic acid. J. Biol. Chem. 134 (1940) 463-464
3. Warburg O., and Christian W. Isolierung und Kristallisation des Proteins des oxydierenden Gärungsferments. Biochem. Z. 303 (1939) 40-48
4. Stadtman E.R., and Barker H.A. Fatty acid synthesis by enzyme preparations of Clostridium kluyveri. VI. Reactions of acyl phosphates. J. Biol. Chem. 184 (1950) 769-793
5. Lynen F., and Holzer H. Über den aeroben Phosphatbedarf der Hefe II. Liebigs Ann. Chem. 563 (1949) 213-239
6. Holzer H., and Holzer E. Bestimmung stationärer Triosephosphatkonzentrationen in lebender Hefe. Beitrag zum Mechanismus des Pasteur-Effektes. Hoppe-Seyler's Z. Physiol. Chem. 292 (1953) 232-239
7. Holzer H., Schultz G., and Lynen F. Bestimmung des Quotienten DPNH/DPN in lebenden Hefezellen durch Analyse stationärer Alkohol- und Acetaldehyd-Konzentrationen. Biochem. Z. 328 (1956) 252-263
8. Holzer H., Haan J., and Pette D. Zusammenhang zwischen Wachstum und aerober Görung. II. Wachstumshemmung des Ehrlich'schen Mäuse-Ascites-Carcinoms mit Jodacetat. Biochem. Z. 327 (1955) 195-201
9. Holzer H., Witt I., and Freytag-Hilf R. Zum Mechanismus des Pasteur-Effektes. Bestimmung von ATP, ADP, Orthophosphat und verschiedenen Zwischenprodukten des Kohlenhydratstoffwechsels in lebenden Hefezellen beim Übergang von anaeroben zu aeroben Bedingungen. Biochem. Z. 329 (1958) 467-475
10. Witt I., Kronau R., and Holzer H. Isoenzyme der Malatdehydrogenase und ihre Regulation in Saccharomyces cerevisiae. Biochim. Biophys. Acta 128 (1966) 63-73
11. Ferguson Jr. J.J., Boll M., and Holzer H. Yeast malate dehydrogenase: enzyme inactivation in catabolite repression. Eur. J. Biochem. 1 (1967) 21-25
12. Gancedo J.M., Atzpodien W., and Holzer H. Stimulation of the protein-dependent interconversion of two forms of yeast phosphofructokinase by a heat-stable fraction from yeast. FEBS Lett. 5 (1969) 199-201
13. Hierholzer G., and Holzer H. Repression der Synthese von DPN-abhängiger Glutaminsäuredehydrogenase in S. cerevisiae durch Ammoniumionen. Biochem. Z. 339 (1963) 175-185
14. Holzer H., and Goedde H.W. Zwei Wege von Pyruvat zu AcetylCoenzym A in Hefe. Biochem. Z. 329 (1957) 175-191
15. Warburg O. Ideen zur Fermentchemie der Tumoren (1947), Abh. Dtsch. Akad. Wiss., Berlin
16. Holzer H., Sedlmayr G., and Kemnitz A. Zum Wirkungsmechanismus carcinostatischer Chemotherapeutika: Hemmung der Glykolyse durch Athyleniminverbindungen. Biochem. Z. 328 (1956) 163-175
17. Holzer H., Glogner P., and Sedlmayr G. Zum Mechanismus der Glykolysehemmung durch carcinostatisch wirkende Athyleniminverbindungen. Biochem. Z. 330 (1958) 59-72
18. Kun E., Langer B., Ulrich B., Holzer H., and Grunicke H. The role of DPNase. The Mechanisms of Action of Antitumor Alkylating Agents on Ehrlich-Ascites Cells. Proc. Natl. Acad. Sci. USA 52 (1964) 1501-1506
19. Holzer H. Action of alkylating substances on glycolysis. In: Plattner R.A. (Ed). Chemotherapy of Cancer (1964), Elsevier, Amsterdam 44-50
20. + in liver mitochondria (protein-bound ADP-ribose/oligo (ADP-ribose)). Proc. Natl. Acad. Sci. USA 72 (1975) 1436-1440
21. Lohmann K., and Schuster P. Cocarboxylase. Biochem. Z. 294 (1937) 188
22. Gunsalus I.C. Group transfer and acyl-generating functions of lipoic acid derivatives. In: McElroy W.D., and Glass B. (Eds). The Mechanism of Enzyme Action (1954), The Johns Hopkins Press, Baltimore, MD 545-562
23. Lynen F., Reichert E., and Rueff L. Zum biologischen Abbau der Essigsäure VI. "Aktivierte Essigsäure", ihre Isolierung aus Hefe und ihre chemische Natur. Liebigs Ann. Chem. 578 (1951) 1-32
24. Holzer H., and Beaucamp K. Nachweis und Charakterisierung von Zwischenprodukten der Decarboxylierung und Oxydation von Pyruvat: "aktiviertes Pyruvat" und "aktivierter Acetaldehyd". Angew. Chem. 71 (1959) 776
25. Breslow R. Mechanism of thiamine action. IV. Evidence from studies on model systems. J. Am. Chem. Soc. 80 (1958) 3719-3726
26. Krampitz L.O., Greull G., Miller C.S., Bicking J.B., Skeggs H.R., and Sprague J.M. An active acetaldehyde-thiamine intermediate. J. Am. Chem. Soc. 80 (1958) 5893-5895
27. Ullrich J., Ostrovsky Y.M., Eyzaguirre J., and Holzer H. Thiamine pyrophosphate-catalyzed enzymatic decarboxylation of α-oxo acids. Vitamins Hormones 28 (1971) 365-398
28. Kohlhaw G., Deus B., and Holzer H. Enzymatic preparation, structure and properties of thiamine pyrophosphate-activated formaldehyde. J. Biol. Chem. 240 (1965) 2135-2141
29. Da Fonseca-Wollheim F., Bock K.W., and Holzer H. Preparation of "active glycolic aldehyde" (2-(1,2-dihydroxyethyl) thiamine pyrophosphate) from hydroxypyruvate and thiamine pyrophosphate with a preparation of pyruvate oxidase from pig heart muscle. Biochem. Biophys. Res. Commun. 9 (1962) 466-471
30. Holzer H. Wirkungsmechanismus von Thiaminpyrophosphat. Angew. Chem. 73 (1961) 721-727
31. +. Biochim. Biophys. Acta 122 (1966) 341-351
32. Ebner E., Wolf D., Gancedo C., Elsässer S., and Holzer H. ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties. Eur. J. Biochem. 14 (1970) 535-544
33. Wulff K., Mecke D., and Holzer H. Mechanism of the enzymatic inactivation of Blutamine synthetase from E. coli. Biochem. Biophys. Res. Commun. 28 (1967) 740-745
34. Holzer H., and Wohlhueter R. (Glutamine synthetase) tyrosylO-adenylate: a new energy-rich phosphate bond. In: Weber G. (Ed). Advances in Enzyme Regulations Vol. 10 (1972), Pergamon Press, Oxford 121-132
35. Shapiro B.M., and Stadtman E.R. 5′-Adenylyl-O-tyrosine. A novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli. J. Biol. Chem. 243 (1968) 3769-3771
36. Heilmeyer Jr. L., Mecke D., and Holzer H. Reaktivierung von Ammonium-inaktivierter Glutaminsynthetase in Escherichia coli. Eur. J. Biochem. 2 (1967) 399-402
37. Betz H., Hinze H., and Holzer H. Isolation and properties of two inhibitors of proteinase B from yeast. J. Biol. Chem. 249 (1974) 4515-4521
38. Holzer H. Characteristics and functions of proteinases and proteinase inhibitors in yeast. In: Shaltiel S. (Ed). Metabolic Interconversion of Enzymes 1975 (1976), Springer-Verlag, Berlin 168-174
39. Müller M., Müller H., and Holzer H. Immunochemical studies on catabolite inactivation of phosphoenolpyruvate carboxykinase in Saccharomyces cerevisiae. J. Biol. Chem. 256 (1980) 723-727
40. Holzer H. Catabolite inactivation in yeast. Trends Biochem. Sci. 1 (1976) 178-181
41. Holzer H., and Heinrich P.C. Control of proteolysis. Annu. Rev. Biochem. 49 (1980) 63-91
42. Holzer H., and Duntze W. Metabolic regulation by chemical modification of enzymes. Annu. Rev. Biochem. 40 (1971) 345-351
43. Afting E.-G., Ruppert D., Hagmaier V., and Holzer H. Yeast phosphofructokinase: effector-controlled conversion of an ATP-sensitive to an ATP-desensitized form. Arch. Biochem. Biophys. 143 (1971) 587-592
44. Lenz A.-G., and Holzer H. Rapid reversible inactivation of fructose-1,6-bisphosphatase in Saccharomyces cerevisiae by glucose. FEBS Lett. 109 (1980) 271-274
45. Tortora P., Birtel M., Lenz A.-G., and Holzer H. Glucosedependent metabolic interconversion of fructose-1,6-bisphosphatase in yeast. Biochem. Biophys. Res. Commun. 100 (1981) 688-695
46. Pohling G., Wingender-Drissen R., Noda T., and Holzer H. Cyclic AMP and fructose-2,6-bisphosphate stimulated in vitro phosphorylation of yeast fructose-1,6-bisphosphatase. Biochem. Biophys. Res. Commun. 115 (1983) 317-324
47. Holzer H., and Purwin C. How does glucose initiate proteolysis of yeast fructose-1,6-bisphosphatase?. Biomed. Biochim. Acta 45 (1986) 1657-1663
48. Horn D., and Holzer H. Phosphorylated fructose-1,6-bisphosphatase dephosphorylating protein phosphatase from Saccharomyces cerevisiae. J. Biol. Chem. 262 (1987) 2056-2061
49. Plankert U., Purwin C., and Holzer H. Yeast fructose-2,6-bisphosphate 6-phosphatase is encoded by PH08, the gene for nonspecific repressible alkaline phosphatase. Eur. J. Biochem. 196 (1991) 191-196
50. Hinze H., and Holzer H. Analysis of the energy metabolism after incubation of Saccharomyces cerevisiae with sulfite or nitrite. Arch. Microbiol. 45 (1986) 27-31
51. Beck-Speier I., Hinze H., and Holzer H. Effect of sulfite on the energy metabolism of mammalian tissues in correlation to sulfite oxidase activity. Biochim. Biophys. Acta 841 (1985) 81-89
52. Nwaka S., and Holzer H. Molecular biology of trehalose and the trehalases in the yeast Saccharomyces cerevisiae (review). Prog. Nucleic Acid Res. Mol. Biol. 58 (1998) 197-237
53. Mittenbühler K., and Holzer H. Characterization of different forms of yeast acid trehalase in the secretory pathway. Arch. Microbiol. 155 (1991) 217-220
54. App H., and Holzer H. Purification and characterization of neutral trehalase from the yeast ABYS1 mutant. J. Biol. Chem. 264 (1989) 17583-17588
55. Kopp M., Nwaka S., and Holzer H. Corrected sequence of the yeast neutral trehalase-encoding gene (nthl): biological implications. Gene 150 (1994) 403-404
56. Destruelle M., Holzer H., and Klionsky D. Isolation and characterization of a novel yeast gene, ATH1, that is required for vacuolar acid trehalase activity. Yeast 11 (1995) 1015-1025