Tryptophanase-catalysed degradation of D-tryptophan in highly concentrated diammonium hydrogen phosphate solution
Tóm tắt
Tryptophanase is and is perfectly inert to D-tryptophan under ordinary conditions. However, activity that can degrade D-tryptophan into indole is observed when tryptophanase is in highly concentrated diammoniumhydrogen phosphate solution. The reaction has been so far unknown in tryptophanase metabolic pathways. Here we report the characteristic of the reaction. We also discuss its significance in relation to selection of an amino acid optical isomer from a racemic mixture.
Tài liệu tham khảo
Alexander FW, Sanmeier E, Mehta PK, Christen P (1994) Evolutionary relationships among pyridoxal 5′-phosphate-dependent enzymes: regio-specific alpha, beta and gamma families. Eur J Biochem 219: 953–960
Behbahani-Nejad I, Dye JL, Suelter CH (1987) Tryptophanase fromEscherichia coli B/1t7-A. Methods Enzymol 142: 414–422
De-Vrese M, Middendorf K, Hagemeister H (1994) Prevention of amino acid racemization during guanidination: prerequisite for measurement of protein digestibility by homoarginine labeling. Z Ernahrungswiss 33: 310–312
Isoyama M, Ohoka H, Kikuchi H, Shimada A, Yuasa S (1984) In vitro protein synthesis using D-amino acids and its evolutionary significance. Orig Life 14: 439–446
Landry J, Delhaye S (1994) The tryptophan contents of wheat, maize and barley grains as a function of nitrogen content. J Cereal Science 18: 259–266
Metzler CM, Viswanath R, Metzler DE (1991) Equilibria and absorption spectra of tryptophanase. J Biol Chem 266: 9374–9381
Mizobata T, Kawabata Y (1995) The folding characteristics of tryptophanase fromEscherichia coli. J Biochemistry 117: 384–391
Shimada A, Nakamura I (1992) Degradation of D-tryptophan under high salt concentration. Viva Origino 20: 147–162
Snell EE (1975) Tryptophanase: structure, catalytic activities, and mechanism of action. Adv Enzymol Relat Areas Mol Biol 42: 287–333
Vanoni MA, Accornero P, Carrera G, Curti B (1994) The pH-dependent behavior of catalytic activities of Azospirillum brasilense glutamate synthase and iodoacetamide modification of the enzyme provide evidence for a catalytic Cys-His ion pair. Arch Biochem Biophys 309: 222–230
Webb EC (1984) Enzyme nomenclature. Academic Press, Inc., Florida, p 20
Yuasa S, Itoh M, Shimada A (1984) Resolution of amino acids by a native-cellulose column. J Chromatogr Sci 22: 288–292