Glycosyl transfer: A history of the concept's development and view of its major contributions to biochemistry

Carbohydrate Research

Volumn 331, Issue 4, 2001, Pages 347-368

  Hehre, Edward J ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL MODIFICATION; GENES; PROTEINS; SYNTHESIS (CHEMICAL);

TRANSGLYCOSYLATION;

BIOCHEMISTRY;

AMINOLEVULINIC ACID; BACTERIAL ENZYME; CARBOHYDRATE; CYCLODEXTRIN; DEXTRAN; DISACCHARIDE; FRUCTOSE; GLUCOSE; GLUCOSE 1 PHOSPHATE; GLUCOSIDE; GLYCOSIDE; GLYCOSYLTRANSFERASE; HEXOSE; LEVAN; PHOSPHATE; POLYSACCHARIDE; SALICIN; STARCH; SUCROSE; WATER;

CARBOHYDRATE SYNTHESIS; GLYCOSYLATION; HYDROLYSIS; PRIORITY JOURNAL; REVIEW;

BIOCHEMISTRY; GLYCOSIDE HYDROLASES; GLYCOSYLATION; GLYCOSYLTRANSFERASES; HISTORY, 19TH CENTURY; HISTORY, 20TH CENTURY; MODELS, BIOLOGICAL; MODELS, CHEMICAL;

EID: 0035938027     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6215(01)00042-8     Document Type: Review

References (248)

1. Chemistry in Medicine; Steglitz, J., Ed.; The Chemical Foundation: New York, 1929; p. 757.
2. Neill J.M., Hehre E.J., Sugg J.Y., Jaffe E. J. Exp. Med. 70:1939;427-442.
3. Neill J.M., Sugg J.Y., Hehre E.J., Jaffe E. Am. J. Hyg. 34:1941;65-78.
4. Sugg J.Y., Hehre E.J. J. Immunol. 43:1942;119-128.
5. Fowler F.L., Buckland I.K., Brauns F., Hibbert H. Can. J. Res. 15B:1937;486-497.
6. Peat, S.; Schlucterer, E.; Stacey, M. J. Chem. Soc. 1939, 581-585.
7. Hassid W.Z., Barker H.A. J. Biol. Chem. 134:1940;163-170.
8. Hill A.C. J. Chem. Soc. 43:1898;634-658.
9. Emmerling O. Chem. Ber. 34:1901;600. 2206-2207, 3810-3811.
10. Hill A.C. Chem. Ber. 34:1901;1380-1384.
11. Hill A. J. Chem. Soc. 83:1903;578-598.
12. Armstrong E.-F. Proc. R. Soc. B. 76:1905;592-599.
13. Fisher E., Armstrong E.-F. Chem. Ber. 35:1902;3144-3153.
14. van't Hoff J.A. Sitz. d. k. Preus. Akad. Wiss. 48:1910;963-970.
15. Visser A.W. Z. Phys. Chem. 52:1905;257.
16. Bayliss W.M. J. Physiol. 43:1911;455-466.
17. Smith R.G., Steel T. J. Soc. Chem. Ind. 21:1902;1381-1385.
18. Lechevelier H.A., Solotorovsky M. Three Centuries of Microbiology. 1965;275-289 McGraw Hill, New York.
19. Beijerinck, M. W. In Koninkl. Acad. v. Wetensch., Proc. Sect. Sci. XII part 2 (English edition); Amsterdam, 1910, pp. 635-640, 795-798.
20. Beijerinck, M. W. Folia Microbiol. 1912, 1, 377-401; Chem. Abstr. 1912, 8, 944.
21. Beijerinck, M. W. Folia Microbiol. 1912, 1, 377-401; Chem. Abstr. 1912, 8, 944.
22. Harrison F.C., Tarr H.L.A., Hibbert H. Can. J. Res. 3:1930;449-463.
23. Dienes L. J. Infect. Dis. 57:1935;22-45.
24. Lwoff A. Burnet F.M., Stanley W.M. The Viruses. 3:1959;1888 Academic, New York.
25. Bourquelot E., Bridel M. J. Pharm. Chim. 5:1912;388-392.
26. Bourquelot E., Bridel M. J. Pharm. Chim. 6:1912;56-62. 97-103, 164-169, 193-199, 298-301, 442-445.
27. Bourquelot E., Bridel M. J. Pharm. Chim. 8:1913;489. 547-553.
28. Bourquelot E., Bridel M., Aubry A. J. Pharm. Chim. 8:1913;411.
29. Bourquelot E. J. Pharm. Chim. 10:1914;361-412.
30. Bourquelot E. Ann. Chim. 3:1915;287.
31. Bourquelot E. Rev. Gen. Sci. 31:1920;745-752.
32. Bourquelot E., Herissey H., Coirre J. C. R. Acad. Sci. 157:1914;732-734.
33. Bourquelot E., Aubry A. J. Pharm. Chim. 14:1916;65-78.
34. Bourquelot E., Bridel M., Aubry A. J. Pharm. Chim. 16:1917;353.
35. Bourquelot, E.; Aubry, A. C. R. Acad. Sci. 1917, 164, 443-445, 521-523; Chem. Abstr. 1917, 11, 1645, 1954.
36. Bourquelot, E.; Aubry, A. C. R. Acad. Sci. 1917, 164, 443-445, 521-523; Chem. Abstr. 1917, 11, 1645, 1954.
37. Bourquelot, E.; Bridel, M. C. R. Acad. Sci. 1919, 168, 253-256, 1016-1019; Chem. Abstr., 1919, 13, 1209-1210.
38. Bourquelot, E.; Bridel, M. C. R. Acad. Sci. 1919, 168, 253-256, 1016-1019; Chem. Abstr., 1919, 13, 1209-1210.
39. Bridel M. Bull. Soc. Chim. Biol. 4:1922;329-354.
40. Rabate J. Bull. Soc. Chim. Biol. 17:1935;572-601.
41. Fleury P., Courtois J.-E. Bull. Soc. Chim. Biol. 41:1959;933-957. esp. 949.
42. Courtois J.-E. Bull. Soc. Chim. Biol. 42:1863;1865. 1960.
43. Rabate J. C. R. Acad. Sci. 204:1937;153-155.
44. Rabate J. Bull. Soc. Chim. Biol. 20:1938;449-453.
45. Rabate J. Baumann E., Myrbäck K. Die Methoden d. Fermentforschung. 5th ed. 1940;1818-1827 Thieme, Leipzig. esp. 1823-1827.
46. Bacon J.S.D. Ann. Rep. Prog. Chem. 50:1954;281-287. esp. 281.
47. Hassid W.Z., Ballou C.E. Pigman W. The Carbohydrates. 1957;478-535 Academic, New York. esp. 528.
48. Stanek J., Černý M., Pacak J. The Oligosaccharides. 1965;122 Czechoslavakia Academy of Science, Prague.
49. Miwa T., Takano K., Mafune K., Furutani S. Proc. Jpn. Acad. 25:1948;111-115.
50. Kalckar H.M. McElroy W.D., Glass B. The Mechanism of Enzyme Action. 1954;675-739 Johns Hopkins, Baltimore. esp. 677.
51. Koshland D.E. Jr., Stein S.S. J. Biol. Chem. 208:1954;139-148.
52. Morton R.K. Discuss. Faraday Soc. 20:1955;149-156. esp. 149.
53. Courtois J.-E., Leclerc M. Bull. Soc. Chim. Biol. 38:1956;365-375.
54. Stone B.A. Long C. Biochemists Handbook. 1961;224 van Nostrand, New York.
55. Courtois J.-E., Perles R. Boulanger P., Polonovski J. Traite de Biochimie Générale. 2:1964;224-395 Masson, Paris. esp. 303.
56. Courtois J.-E., Percheron F. Pigman W., Horton D. The Carbohydrates. 2nd ed. 1970;213-240 Academic, New York.
57. Dedonder R. Ann. Rev. Biochem. 30:1961;347-382. esp. 347.
58. Bourne, E. J.; Macey, A.; Peat, S. J. Chem. Soc. 1945, 882-888.
59. Peat S., Bourne E.J., Barker S. Nature. 161:1948;127-128.
60. Parnas J.K., Baranowski T. C. R. Soc. Biol. 120:1935;307-310.
61. Parnas J.-K. Ergeb. Enzymforsh. 6:1937;57-110. esp. 69, 81-82.
62. Cori C.F., Cori G.T. Proc. Soc. Exp. Biol. Med. 34:1936;702-705.
63. Cori C.F., Colowick S.P., Cori G.T. J. Biol. Chem. 123:1938;375-380.
64. Cori G.T., Colowick S.P., Cori C.F. J. Biol. Chem. 123:1938;381-389.
65. Kiessling W. Naturwissenschaften. 27:1939;129-130.
66. Kiessling W. Biochem. Z. 302:1939;50-72.
67. Schäffner A., Specht H. Naturwissenschaften. 26:1938;494-495.
68. Cori, C. F.; Schmidt, H.; Cori, G. T. Science 1939, 464-465.
69. Cori G.T., Cori C.F., Schmidt G. J. Biol. Chem. 129:1939;629-639.
70. Cori G.T., Cori C.F. J. Biol. Chem. 131:1939;397-398.
71. Cori G.T., Cori C.F. J. Biol. Chem. 135:1940;733-756.
72. Ostern P., Holmes E. Nature. 144:1939;34.
73. Hanes C.S. Nature. 145:1940;348-349.
74. Hanes C.S. Proc. R. Soc. (Lond.). B129:1940;174-208.
75. Freudenberg, K.; Schaaf, E.; Dumpert, G.; Ploetz, T. Naturwissenschaften 1939, 27, 850-853; Chem. Abstr. 1940, 34, 2632.
76. Freudenberg, K.; Schaaf, E.; Dumpert, G.; Ploetz, T. Naturwissenschaften 1939, 27, 850-853; Chem. Abstr. 1940, 34, 2632.
77. Tilden E.B., Hudson C.S. J. Am. Chem. Soc. 61:1939;2900-2902.
78. Hanes C.S. New Phytol. 36:1937;189-239.
79. Kuhn R., Dansi A. Ber. Deutsch. Chem. Ges. 69:1936;1745-1754.
80. Tilden E.B., Hudson C.S. J. Bact. 43:1942;527-544.
81. Tilden E.B., Hudson C.S. J. Am. Chem. Soc. 64:1942;1432-1433.
82. McClenehan W.S., Tilden E.B., Hudson C.S. J. Am. Chem. Soc. 64:1942;2139-2144.
83. Kerr R.W. J. Am. Chem. Soc. 64:1942;3044-3045.
84. French D., Rundle R.E. J. Am. Chem. Soc. 64:1942;1651-1653.
85. Wilson E.J. Jr., Schoch T.J., Hudson C.S. J. Am. Chem. Soc. 65:1943;1380-1383.
86. Meyer K.H. Adv. Enzymol. 3:1943;109-135.
87. Cori C.F. Fed. Proc. 4:1945;226.
88. Myrbäck K., Györling L.-G. Arkiv Kemi., Minerol., Geol. A20:1945;1-13. esp. 2.
89. Myrbäck K., Järneström T. Arkiv. Kemi. 1:1948;129-143. esp. 129-130.
90. Myrbäck K. Adv. Carbohydr. Chem. 3:1948;252-310.
91. French D., Pazur J., Levine M.L., Norberg E. J. Am. Chem. Soc. 70:1948;3145.
92. Barker, S. A.; Bourne, E. J. Q. Rev. Chem. Soc. 1963, VII, 56-83, esp. 64.
93. French D. Adv. Carbohydr. Chem. 12:1957;189-260. esp. 225.
94. Hassid W.Z. Fed. Proc. 4:1945;227-241.
95. Clarke R.J., Coates J.H., Lincoln S.F. Adv. Carbohydr. Chem. Biochem. 46:1988;205-249. esp. 215-217.
96. Hehre E.J. Adv. Enzymol. 11:1951;297-337.
97. Hehre E.J., Mizokami K., Kitahata S. Dempun Kagaku (Jpn. J. Starch Sci.). 30:1983;76-82.
98. Miwa, T.; Mafune, K.; Furuya, T. Igaku to Seibutsugaku (Medicine Biol.) 1942, 1, 80-84 (in Japanese). Nisizawa K. Sorui (Jpn. J. Phycol.) 1980, 28, 201-204.
99. Miwa, T.; Mafune, K.; Furuya, T. Igaku to Seibutsugaku (Medicine Biol.) 1942, 1, 80-84 (in Japanese). Nisizawa K. Sorui (Jpn. J. Phycol.) 1980, 28, 201-204.
100. Hehre E.J. Science. 93:1941;237-238.
101. Hehre E.J., Sugg J.Y. J. Exp. Med. 75:1942;339-353.
102. Stacey M. Nature. 149:1942;639.
103. Hestrin S., Avineri-Shapiro S. Biochem. J. 38:1944;2-10.
104. Lineweaver H., Jansen A.F. Ann. Rev. Biochem. 14:1945;69-90.
105. Doudoroff M. Fed. Proc. 4:1945;241-247.
106. Kalckar H.M. Nature. 160:1947;143-147.
107. Hassid W.Z., Doudoroff M. Adv. Carbohydr. Chem. Biochem. 5:1950;29-48.
108. Stodola F.H. Chemical Transformations by Microorganisms. 1971;71 Wiley, New York.
109. Mooser G. The enzymes. Sigman D.S. 3rd ed. Mechanisms of Catalysis. 20:1992;210 Academic, New York.
110. Kagan B.O., Latker S.N., Zfasman E.M. Biokhimiya. 7:1942;93-108. (In Russian).
111. Hehre E.J. Proc. Soc. Biol. Med. 54:1943;240-241.
112. Schramm M. Bull. Res. Counc. Isr. IIA:1963;243-244. (Issue dedicated to the memory of Professor Shlomo Hestrin).
113. Hestrin S., Avineri-Shapiro S., Aschner M. Biochem. J. 37:1943;450-456.
114. Hestrin S., Avineri-Shapiro S. Nature. 152:1943;49-50.
115. Hestrin S. Nature. 154:1944;581.
116. Sumner J.B., Summers G.F. Chemistry and Methods of Enzymes. 2nd ed. 1947, xiv;Academic, New York.
117. Evans T.H., Hibbert H. Adv. Carbohydr. Chem. 2:1946;204-233.
118. Whistler R.L., Smart C.L. Polysaccharide Chemistry. 1953;378, 385 Academic, New York.
119. Haworth, W. N.; Heath, R. L.; Peat, S. J. Chem. Soc. 1942, 55-58.
120. Green A.A., Cori G.T., Cori C.F. J. Biol. Chem. 142:1942;447-448.
121. Green A.A., Cori G.T., Cori C.F. J. Biol. Chem. 151:1943;21-29.
122. Hassid W.Z., Cori G.T., McCready R.M. J. Biol. Chem. 148:1943;89-96.
123. Cori G.T., Cori C.F. J. Biol. Chem. 151:1943;57-63.
124. Doudoroff M., Kaplan N., Hassid W.Z. J. Biol. Chem. 148:1943;67-75.
125. Doudoroff M. J. Biol. Chem. 151:1943;351-361.
126. Hassid W.Z., Doudoroff M., Barker H.A. J. Am. Chem. Soc. 66:1944;1416-1419.
127. Hudson C.S. J. Am. Chem. Soc. 30:1908;1564-1583.
128. Weidenhagen R. Ergeb. Enzymforsch. 2:1933;90-103.
129. Lemieux R.U., Huber G. J. Am. Chem. Soc. 78:1956;4117-4119.
130. Doudoroff M., Hassid W.Z., Barker H.A. Science. 100:1944;315-316.
131. Kalckar H.M. Fed. Proc. 4:1945;248-252.
132. Kalckar H.M. J. Biol. Chem. 167:1947;477-486.
133. Doudoroff M. Fed. Proc. 4:1945;241-247.
134. Hassid W.Z., Doudoroff M., Barker H.A., Dore W.H. J. Am. Chem. Soc. 67:1945;1465-1467.
135. Raybin H.W. J. Am. Chem. Soc. 55:1933;2603-2604.
136. Raybin H.W. J. Am. Chem. Soc. 59:1937;1402-1403.
137. Hehre E.J. J. Biol. Chem. 163:1946;221-233.
138. Hehre E.J., Hamilton D.M. J. Biol. Chem. 166:1946;777-778.
139. Doudoroff M., Barker H.A., Hassid W.Z. J. Biol. Chem. 168:1947;725-732.
140. Koshland D.E. Jr. Biol. Rev. Cambridge Phil. Soc. 28:1953;416-436.
141. Koshland D.E. Jr. McElroy W.D., Glass B. The Mechanism of Enzyme Action. 1954;608-641 John Hopkins, Baltimore.
142. Doudoroff M., O'Neal R. J. Biol. Chem. 159:1945;585-592.
143. Bell D.J. Ann. Rep. Chem. Soc. 44:1947;2l7-226.
144. Hassid W.Z., Doudoroff M. Fortschr. Chem. Org. Naturstoffe. 5:1948;101-127.
145. Hestrin S. Brewer's Digest. 23:1948;1-4. 8.
146. Hehre E.J. Trans. New York Acad. Sci., Ser. 11. 10:1948;188-198.
147. Hehre E.J., Hamilton D.M. J. Bact. 55:1948;197-208.
148. Hehre E.J., Hamilton D.M., Carlson A.S. J. Biol. Chem. 177:1949;267-279.
149. Monod J., Torriani A.-M. C. R. Acad. Sci. 227:1948;240-241.
150. Torriani A.-M., Monod J. C. R. Acad. Sci. 228:1949;718-720.
151. Doudoroff M., Hassid W.Z., Putman E.W., Potter A.L., Lederberg J. J. Biol. Chem. 179:1949;921-934.
152. Hassid W.Z., Doudoroff M., Barker H.A. Arch. Biochem. Biophys. 14:1947;29-37.
153. Cohn M. J. Biol. Chem. 180:1949;771-781.
154. Myrbäck K., Neumüller G. Sumner J.B., Myrbäck K. The Enzymes, Part 1. 1:1950;653-724 Academic, New York.
155. Barker, S. A.; Bourne, E. J.; Peat, S. J. Chem. Soc. 1949, 1712-1716.
156. Peat S. Adv. Enzymol. 11:1951;339-375.
157. Larner J. J. Biol. Chem. 202:1953;491-503.
158. Bacon J.S.D., Edelman J. Arch. Biochem. Biophys. 28:1950;467-468.
159. Blanchard P.H., Albon N. Arch. Biochem. Biophys. 29:1950;220-222.
160. Takano K., Miwa T. J. Biochem. 37:1950;435-444.
161. Fisher E.H., Kohtes J., Fellig J. Helv. Chim. Acta. 34:1951;1132-1138.
162. Wallenfels K. Naturwissenschaften. 38:1951;306-307.
163. Pazur J.H., French D. J. Biol. Chem. 196:1952;265-272.
164. Whitby L.G. Biochem. J. 50:1952;433-438.
165. Pazur J.H. J. Biol. Chem. 199:1952;217-225.
166. Aronson M. Arch. Biochem. Biophys. 39:1952;370-378.
167. Pan S.C., Nicholson L.W., Kolachov P. Arch. Biochem. Biophys. 42:1953;406-420.
168. White J.W. Jr., Maher J. Arch. Biochem. Biophys. 42:1953;360-367.
169. Wallenfels K., Bernt E. Liebigs Ann. 584:1953;63-85.
170. Roberts H.R., McFarren E.F. Arch. Biochem. Biophys. 43:1953;233-234.
171. Pazur J.H. J. Am. Chem. Soc. 75:1953;6323-6324.
172. Takano K., Miwa T. J. Biochem. 40:1953;471-476.
173. Giri K.V., Narasimha Rao P.L., Saroja K., Venkataraman R. Naturwissenschaften. 40:1953;484-485.
174. Giri K.V., Nigam V.N., Srinivasan K.S. Nature. 173:1954;953-954.
175. Giri K.V., Nagabhushanam A., Nigam V.N., Belavadi B. Science. 121:1955;898-899.
176. Miwa T., Takano K., Mafune K., Furutani S. Proc. Jpn. Acad. 25:1949;111-115.
177. Miller K.D., Copeland W.H. Biochim. Biophys. Acta. 22:1956;193-194.
178. Miwa T., Takano K., Yasumura A., Suzuki H., Isizawa K. Symp. Enzyme Chem. (Jpn.). 11:1956;225-232.
179. Suzuki H. Sci. Rep., Toyko Kyoiku Daigaku, Sect. B. 8:1957;80-94.
180. Sawai T. J. Biochem. 45:1958;50-56.
181. Miller K.D. J. Biol. Chem. 231:1958;987-995.
182. Miller K.D., Copeland W.H. J. Biol. Chem. 231:1958;999-1008.
183. Stetten M.R. J. Am. Chem. Soc. 81:1959;1437-1447.
184. Petrova A.N. Enzymologia. 21:1959;23-31.
185. Miwa T., Takeshita M., Nakamura S. Biochim. Biophys. Acta. 37:1960;541-542.
186. Matsubara S. J. Biochem. 49:1961;226-231.
187. Sawai, T.; Hehre, E. J. Bacteriol. Proc. 1960, 161; J. Biol. Chem. 1962, 237, 2047-2052.
188. Sawai, T.; Hehre, E. J. Bacteriol. Proc. 1960, 161; J. Biol. Chem. 1962, 237, 2047-2052.
189. Hassid W.Z., Doudoroff M. Adv. Carbohydr. Chem. 5:1950;29-48.
190. 105.
191. Hassid W.Z., Doudoroff M., Barker H.A. Sumner J.B., Myrbäck K. Enzymes, Part 2. 1:1951;1014-1039 Academic, New York.
192. Hassid W.Z. McElroy W.D., Glass B. Phosphorus Metabolism. 1:1951;11-42 Johns Hopkins, Baltimore.
193. Pictet A., Castan P. Helv. Chim. Acta. 4:1921;319-324.
194. American Chemical Society, Committee Report on Rules of Carbohydrate Nomenclature. Chem. Eng. News 1948, 26, 1623-1626.
195. Cohn M. Pychior H.M., Slack N.G., Abir-Am P.G. Creative Couples in the Sciences. 1996;72-84 Rutgers University, New Brunswick, NJ. 304-305.
196. Ballou C., Barker H.A. Natl. Acad. Sci. 50:1979;187-230.
197. French D., Levine M.L., Norberg E., Nordin P., Pazur J.H., Wild G.M. J. Am. Chem. Soc. 76:1954;2387-2390.
198. Hassid W.Z. Greenberg D. 1st ed. Chemical Pathways of Metabolism. 1:1954;235-275 Academic, New York. esp. 245, 251.
199. Bourne, E. J.; Biochemistry Society Symposium no. II; Cambridge University, 1953; pp. 3-16.
200. Bacon J.S.D. Ann. Rep. Progr. Chem. 50:1954;28l-287.
201. Hoffmann-Ostenhof O. Adv. Enzymol. 14:1953;219-260.
202. Hehre E.J. J. Biol. Chem. 192:1951;161-174.
203. Hestrin S. Goodwin T.W., Lindberg O. Biological Structure and Function. 1:1961;315-325 Academic, London.
204. Hestrin S., Feingold D.S., Avigad G. Biochem. J. 64:1956;340-351.
205. Miwa T. (Tampaku, Kakusan, Kohso (Protein, Nucleic Acid and Enzyme). 2:1957;35-41. (in Japanese).
206. Whistler R.L., Corbett W.M. Pigman W. The Carbohydrates. 1957;641-708 Academic, New York. esp. 703.
207. Leloir L.F., Cardini C.E., Cabib E. Florkin M., Mason H.S. Comparative Biochemistry. 2:1960;97-138 Academic, New York.
208. Hassid W.Z., Neufeld E.F. Boyer P.D., Lardy H., Myrbäck K. The Enzymes. 6:1962;277-315 Academic, New York.
209. Pazur, J. H. In Starch: Chemistry and Technology; Whistler, R.; Paschall, E. F., Eds.; Academic: New York, 1965; pp. 133-173.
210. Hassid, W. Z. In The Structure and Bisynthesis of Macromolecules; Bell, D. J.; Grant J. K., Eds.; Biochemical Society Symposia, No. 21, 1962; pp. 63-79, esp. 64.
211. Hassid W.Z. Greenberg D.M. 3rd ed. Metabolic Pathways. 1:1967;307-393 Academic, New York. esp. 315.
212. Florkin M. Florkin M., Stotz E.H. Comparative Biochemistry. 33A:1979;141-169 Elsevier, New York. esp. 143.
213. Dedonder R. Piras R., Pontes H.G. Biochemistry of the Glycosidic Linkage. 1972;23 Academic, New York.
214. Leloir L.F., Cabib E. J. Am. Chem. Soc. 75:1953;5445.
215. Cabib E., Leloir L.F. J. Biol. Chem. 231:1958;259-275.
216. Leloir, L. F.; Cardini, C. E. J. Am. Chem. Soc. 1953, 75, 6084.
217. Leloir L.F., Cardini C.E., Chiriboga J. J. Biol. Chem. 214:1955;149-155.
218. Cardini C.E., Leloir L.F. J. Biol. Chem. 214:1955;157-165.
219. Feingold D.S., Neufeld E.F., Hassid W.Z. J. Biol. Chem. 233:1958;783-788.
220. Kornberg S.R., Zimmerman S.B., Kornberg A. J. Biol. Chem. 236:1961;1487-1493.
221. Josse J., Kornberg A. J. Biol. Chem. 237:1962;1968-1972.
222. Lieberman I., Kornberg A., Simms E.S. J. Biol. Chem. 215:1955;403-415.
223. Kornberg A. Adv. Enzymol. 18:1957;191-237.
224. Lehman I.R., Bessman M.J., Simms E.S., Kornberg A. J. Biol. Chem. 233:1958;163-170.
225. Schachman H.K., Adler J., Radding C.M., Lehman I.R., Kornberg A. J. Biol. Chem. 235:1960;3242-3253.
226. Koshland D.E. Jr. Boyer P.D., Lardy H., Myrbäck K. 2nd ed. The Enzymes. 1:1959;305-346 Academic, New York.
227. Bunton C.A., Lewis T.A., Llewellyn D.R., Tistram H., Vernon C.A. Nature. 174:1954;560.
228. Hehre E.J. Bull. Soc. Chim. Biol. 42:1960;1713-1714.
229. Hehre E.J., Genghof D.S., Okada G. Arch. Biochem. Biophys. 142:1971;382-393.
230. Hehre E.J., Okada G., Genghof D.S. Carbohydrates in solution. Gould R.F. Advanced Chemical Series. 117:1973;309-333.
231. IUPAC Commission on the Nomenclature of Organic Chemistry (CNOC) and IUPAC-IUB Commission on Biochemical Nomenclature (CBN). Eur. J. Biochem. 1971, 21, 455-477.
232. IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (JCBN). Adv. Carbohydr. Chem. Biochem. 1997, 52, 1-90.
233. Sinnott M.L. Page M.I. The Chemistry of Enzyme Action. 1984;389-431 Elsevier, Amsterdam.
234. Hehre E.J. Denpun Kagaku (Jpn. J. Starch Sci.). 36:1989;197-205.
235. Hehre, E. J. In Enzymatic Degradation of Insoluble Carbohydrates; Saddler, J. N.; Penner, M. H., Eds.; ACS Symposium Series 618; American Chemical Society: Washington, DC, 1995; pp. 66-78.
236. Sinnott M.L. Page M.I., Williams A. Enzyme Mechanisms. 1987;259-287 Royal Society of Chemistry, London.
237. Sinnott M.L. Chem. Rev. 90:1990;1171-1202.
238. Legler G. Adv. Carbohydr. Chem. Biochem. 48:1990;319-384.
239. Chiba, S. In Enzyme Chemistry and Molecular Biology of Amylases and Related Enzymes; Amylase Research Society of Japan, Ed.; CRC: Tokyo, 1994; pp. 68-82.
240. Davies G., Sinnott M.L., Withers S.G. Sinnott M.L. Comprehensive Biological Catalysis. 1:1998;119-209 Academic, New York.
241. Lougheed B., Ly H.D., Wakarchuk W.W., Withers S.G. J. Biol. Chem. 274:1999;37717-37722.
242. Vrielink A., Rüger W., Driessen H.P.C., Freemont P.S. EMBO J. 13:1994;3413-3422.
243. Morera S., Imberty A., Aschke-Sonnenborn U., Rüger W., Freemont P.S. J. Mol. Biol. 292:1999;717-730.
244. Charnock S.J., Davies G.J. Biochemistry. 38:1999;6380-6385.
245. Gastinel L.N., Cambillau C., Bourne Y. EMBO J. 18:1999;3546-3557.
246. Ha S., Walker D., Shi Y., Walker S. Protein Sci. 9:2000;1045-1052.
247. Ünligel U.M., Rini J.M. Curr. Opin. Struct. Biol. 10:2000;510-517.
248. Hehre, E. J. Adv. Carbohydr. Chem. Biochem. 1999, 55, 265-310; Abstr 214th National Meeting of the American Chemical Society: Las Vegas, NV, September 8, 1997; CARB 5.