Ѕиологический каталог

Ѕиоорганическа€ хими€

јвтор √.ƒюга,  .ѕенни

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284. Jones J. ¬., Beck J. F. Application of Biochemical Systems in Organic Chemistry, In: Techniques of Chemistry Series (J. B. Jones, C. J. Sih, D. Perlman, Eds.), Part I, pp. 107Ч401. Wiley, New York, 1976.

285. Prelog V. Specification of the stereochemistry of some oxidoreductases by diamond lattice sections. Pure Appl. Chem. 9, 119Ч130 (1964).

286. Creighton D. J., Hajdu J., Mooser G., Sigman D. S. Model dehydrogenase reactions. Reduction of N-methylaeridinium ion by reduced nicotinamide adenine dinucleotide and its derivatives. J. Amer. Chem. Soc. 95, 6855Ч6867 (1973).

287. Brilstlein M., Bruice “. C. Demonstration of a direct hydrogen transfer between NADH and a deazaflavin. J. Amer. Chem. Soc. 94, 6548Ч6549 (1972).

288. Fisher J., Walsh C. Enzymatic reduction of 5-deazariboflavine from reduced nicotinamide adenine dinucleotide by direct hydrogen transfer. J. Amer. Chem. Soc. 96, 4345Ч4346 (1974).

289. Eirich D., Vogels G., Wolfe R. Proposed structure of coenzyme F420 from Methanobacterium. Biochemistry 17, 4583Ч4593 (1978).

290. Hemmerich P., Massey V., Weber G. Photo-induced benzyl substitution of flavins by phenylacetate: A possible model for Havoprotein catalysis. Nature 213, 728Ч730 (1967).

291. Sayer J. M., Conlon P., Hupp J., Fancher J., Belanger R., White E. I. Reduction of l,3-dimethyl-5-(p-nitrophenylimino) barbituric acid by thiols. A high-velocity flavin model reaction with an isolable intermediate. J. Amer. Chem. Soc. 101, 1890Ч1893 (1979).

292. Rastetter W. H., Gadek T. R., Tone J. P., Frost J. W-. Oxidations and oxygen transfer effected by a flavin N(5)-oxide. A model for flavin-dependent mono oxygenases. J. Amer. Chem. Soc. 101, 2228Ч2231 (1979).

293. Orf H. W., Dolphin D. Oxaziridines as possible intermediates in flavin mono oxygenases. Proc. Nat. Acad. Sci. USA 71, 2646Ч2650 (1974).

294. Vargo D., Jams M. S. Synthesis of a 4a,5-epoxy-5-deazaflavin derivatives J. Amer. Chem. Soc. 101, 7623Ч7626 (1979).

295. Jerina D. M., Daly J. W., Witkop ¬., Zaltzman-Nirenberg S., Udenfriend S. 1,2-Naphthalene oxide as an intermediate in the microsomal hydroxylation of naphthalene. Biochemistry 9, 147Ч156 (1969).

296. Guroff G., Daly J. W., Jerina D. M., Rensen J., Witkop ¬., Udenfriend S Hydroxylation-induced migration: The NIH shift. Science 157,1524Ч1530 (1967).

297. Fox J. L. Chemists attack complex organic mechanisms. Chem. Eng. News May 22, pp. 28Ч30 (1978).

298. Adam W., Alzerreca A., Liu J. E., Yany F. a-Peroxylactones via dehydrative cyclization of a-hydroperoxy acids. J. Amer. Chem. Soc. 99, 5768Ч5773 (1977).

299. Kemal C., Bruice “. C. Simple synthesis of a 4a-hydroperoxy adduct ol 1,5-dihydroflavine: Preliminary studies of a model for bacterial luciferase. Proc. Nat. Acad. Sci. USA 73, 995Ч999 (1976).

300. Schmidt S. P., Schuster G. B. Dioxetanone chemiluminescence by the chemically initiated electron exchange pathway. Efficient generation of excited singlet states. J. Amer. Chem. Soc. 100, 1966Ч1968 (1978).

301. Lowe J. N., Ingraham L. L. An Introduction to Biochemical Reactions Mechanisms, Chap. 3. Foundation of Molecular Biology Series. Prentice-Hall, Eng-lewood Cliffs, New Jersey, 1974.



302. Gansow ќ. A., Holm R. ». A proton resonance investigation of equilibra, solute structures, and transamination in the aqueous systems pyridoxamine-pyruvate-zinc(II) and aluminium (III). J. Amer. Chem. Soc. 91, 5984Ч5993 (1969).

B03. Blum M., Thanassi J. W. Metal ion induced reaction specific in vitamin B6 model systems. Bioorg. Chem. 6, 31Ч41 (1977).

B04. Belleau ¬., Burba I. The stereochemistry of the enzymic decarboxylation of amino acids. J. Amer. Chem. Soc. 82, 5751Ч5752 (1960).

|S05. Dunathan H. C., Davis L., Kury P. G., Kaplan M. The stereochemistry of enzymatic transamination. Biochemistry 7, 4532Ч4536 (1968).

1306. Dunathan H. C., Voet I. G. Stereochemical evidence for the evolution of pyridoxal-phosphate enzymes of various function from a common ancestor. Proc. Nat. Acad. Sci. USA, 71, 3888Ч3891 (1974).

fe07. Roitenan J. N-, Cram D. J. Electrophilic substitution at saturated carbon. XLV. Dissection of mechanisms of base-catalyzed hydrogen-deuterium exchange of carbon acids into inversion, isoinversion, and racemization pathways. J. Amer. Chem. Soc. 90 ,2225Ч2230 (1971).

B08. Roitenan J. N., Cram D. J. Electrophilic substitution at saturated carbon. XLVI. Crown ethers' ability to alter role of metal cations in control of stereochemical fate of carbanions. J. Amer. Chem. Soc. 90, 2231Ч2241 (1971).

B09. Cram D. J., Ford W. “., Gosser L. Electrophilic substitution and saturated carbon. XXXVIII. Survey of substituent effects on stereochemical fate of fluorenyl carbanions. J. Amer. Chem. Soc. 90, 2598Ч2606 (1968).

B10. Broadhurst M. D., Cram D. J. A model for the proton transfer stages of the biological transaminations and isotopic exchange reactions of amino acids. J. Amer. Chem. Soc. 96, 581Ч583 (1974).

fell. Jaeger D. A., Broadhurst M. D., Cram D. J. Electrophilic substitution at saturated carbon. 52. A model for the proton transfer steps of biological transamination and the effect of a 4-pyridyl group on the base-catalyzed racemization of a carbon acid. J. Amer. Chem. Soc. 101, 717Ч732 (1979).

¬12. Baker B. R. Design of Active-Site-Directed Irreversible Enzyme Inhibitors. Wiley, New York, 1967.

B13. Abeles R. H., Maycock A. L. Suicide enzyme inactivators. Acc. Chem. Res. 9, 313Ч319 (1976).

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the active center of chymotrypsin. Biochemistry 2, 252Ч255 (1963). 315. Walsh C. Chemical approaches to the study of enzymes catalyzing redox

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B20. Fasella P., John R. Substrate analogues as specific inhibitors of pyridoxal-dependent enzymes. Proc. 4th Int. Congr. Pharmacol. 5, 184Ч186 (1969).

321. Morino Y., Okamoto M. Labeling of the active site of cytoplasmic aspartate amino transferase by R-chloro-L-alanine. Biochem. Biophys. Res. Commun. 50, 1061Ч1067 (1973).

322. lung M. J., Metcalf B. W. Catalytic inhibition of y-aminobutyric acid a-keto-glutarate transaminase of bacterial origin by 4-aminohex-5ynoic acid, a substrate analog. Biochem. Biophys. Res. Commun. 67, 301Ч306 (1975).

323. Rando R. R., de Mairena J. Propargyl amine-induced irreversible inhibition of non-flavin-linked amine oxidases. Biochem. Pharmacol. 23, 463Ч466 (1974).

[324. Breslow R. On the mechanism of thiamine action. IV. Evidence from studies on model systems. J. Amer. Chem. Soc. 80, 3719Ч3726 (1958).



325. Gatlo A. A., Sable Ќ. Z. Coenzyme interactions. VIII. 13C-NMR studies of thiamine and related compounds. J. Biol. Chem. 249, 1382Ч1389 (1974).

326. Jordan F., Mariam Y. H. W-Methylthiaminium diiodide. Model study on the effect of a coenzyme bound positive charge on reaction mechanism requiring thiamine pyrophosphate. J. Amer. Chem. Soc 100, 2534Ч2541 (1978).

327. White F., Ingraham L. L. Mechanism of thiamine action: A model of 2-acyl-thiamine. J. Amer. Chem. Soc. 84, 3109Ч3111 (1962).

328. Bruice “. C, Benkovic S. Bioorganic Mechanisms. Vol. 2, Chap. 8, p. 217 Benjamin, New York, 1966.

329. Rastetter W. H., Adams J., Frost J. W., Nummy L. J., Frommer J. ?., Roberts  . B. On the involvement of lipoic acid in a-keto acid dehydrogenase complexes. J. Amer. Chem. Soc. 101, 2752Ч2753 (1979).

330. Bruice “. C, Hegarty A. F. Biotin-bound C02 and the mechanism of enzymatic carboxylation reactions. Proc. Nat. Acad. Sci. USA 65, 805Ч809 (1970).

331. Caplow M., Yager M. Studies on the mechanism of biotin catalysis. H.J. Amer. Chem. Soc. 89, 4513Ч4521 (1976).

332. Guchhait R. ¬., Polakis S. E., Hollis D., Fenselau C., Lane M. D. Acetyl coenzyme A carboxylase system of E. coli. Site of carboxylation of biotin and enzymatic reactivity of I'-N-(ureido)-carboxybiotin derivatives. J. Biol. Chem. 249, 6646Ч6656 (1974).

333. Whitney P. A., Cooper T. G. Urea carboxylase and allophanate hydroxylase Two components of ATP: Urea-lyase in 5. cerevisiae. J. Biol. Chem. 247, 1349Ч1353 (1972).

334. Kluger R., Davis P., Adawadkar P. D. Mechanism of urea participation in phosphonate ester hydrolysis. Mechanistic and stereochemical criteria for enzymic formation and reaction of phosphorylated biotin. J. Amer. Chem. Soc. 101, 5995Ч6000 (1979).

335 Arigoni D., Lynen F., Retey J. Stereochemie der enzymatischen Carboxylie-rung von (2R)-2-3H-Propionyl-CoA. Helv. Chim. Acta 49, 311Ч316 (1966).

336. Retey J., Lynen F. Zur biochemischen Funktion des Biotins. IX Der steri-sche Verlauf der Carboxylierung von Propionyl-CoA. Biochem. Z 342, 256Ч 271 (1965).

337. Kluger R., Pike D. C. Chemical synthesis of a proposed enzymegenerated Ђreactive intermediate analogue* derived fiom thiamine diphosphate. Self-activation of pyruvate dehydrogenase by conversion of the analogue in its components. J. Amer. Chem. Soc. 101, 6425Ч6428 (1979).

338. Moss /., Lane M. D. The biotin-dependent enzymes. Adv. Enzymol. 35, 321Ч442 (1971).

339. Wood H. G., Burden R. E Biotin enzymes. Annu. Rev. Biochem. 46, 385Ч413 (1977).

340. Mildvan A. S. Magnetic resonance studies of the conformations of enzyme-bound substrates. Acc. Chem. Res. 10, 246Ч252 (1977).

341. Klu

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