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An increase in apparent affinity for sucrose of mung bean [Vigna radiata] sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11

Nakai, T. (Kyoto Univ., Uji (Japan). Wood Research Inst.) ; Konishi, T ; Zhang, X.Q ; Chollet, R ; Tonouchi, N ; Tsuchida, T ; Yoshinaga, F ; Mori, H ; Sakai, F ; Hayashi, T

Plant and cell physiology, 1998-12, Vol.39 (12), p.1337-1341 [Periódico revisado por pares]

Oxford: Oxford University Press

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Título:
An increase in apparent affinity for sucrose of mung bean [Vigna radiata] sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11
Autor: Nakai, T. (Kyoto Univ., Uji (Japan). Wood Research Inst.) ; Konishi, T ; Zhang, X.Q ; Chollet, R ; Tonouchi, N ; Tsuchida, T ; Yoshinaga, F ; Mori, H ; Sakai, F ; Hayashi, T
Assuntos: ACTIVADOR ENZIMATICO ; ACTIVATEUR D'ENZYME ; Agronomy. Soil science and plant productions ; Amino Acid Sequence ; Aspartic Acid - genetics ; BIOCHEMICAL REACTIONS ; Biological and medical sciences ; Directed mutagenesis ; Economic plant physiology ; ENZYME ACTIVATORS ; Enzymes ; EXPERIMENTACION IN VITRO ; EXPERIMENTATION IN VITRO ; Fabaceae - enzymology ; FOSFORILACION ; Fundamental and applied biological sciences. Psychology ; Glucosyltransferases - genetics ; Glucosyltransferases - metabolism ; IN VITRO EXPERIMENTATION ; Kinetics ; LIASAS ; LYASE ; LYASES ; Metabolism ; Molecular Sequence Data ; MUTACION ; Mutagenesis, Site-Directed ; MUTATION ; Nutrition. Photosynthesis. Respiration. Metabolism ; PHOSPHORYLATION ; Plant physiology and development ; Plants, Medicinal ; Protein phosphorylation ; Protein Processing, Post-Translational ; REACCIONES BIOQUIMICAS ; REACTION BIOCHIMIQUE ; SACCHAROSE ; Serine - genetics ; Substrate Specificity ; SUCROSA ; SUCROSE ; Sucrose - metabolism ; Sucrose synthase ; VIGNA RADIATA ; Vigna radiata Wilczek
É parte de: Plant and cell physiology, 1998-12, Vol.39 (12), p.1337-1341
Notas: F61
F30
1999003668
istex:91577E26C07CD743E1B15502A571F8DE8AE8198F
ArticleID:39.12.1337
ark:/67375/HXZ-X7S7N97H-P
Descrição: A mutational analysis of mung bean (Vigna radiata Wilczek) sucrose synthase was performed by site-directed mutagenesis of the recombinant protein expressed in Escherichia colt, in which two different acidic amino acid residues (Asp or Glu) were introduced at Ser(11) (S11D, S11E). Only the wild-type enzyme (Ser(11)) was phosphorylated in vitro by a Ca(2+)-dependent protein kinase from soybean root nodules, suggesting that this is the specific target residue in mung bean sucrose synthase. The apparent affinity for sucrose was increased in this phosphorylated enzyme and also in the S(11)D and S11E mutant enzymes, although the affinities for UDP-glucose and fructose were similar in the wild-type, phosphorylated wild-type, and mutant enzymes. These results suggest that a monoanionic (1-) side chain at position 11 mimics the Ser(11)-P(2-) residue to bind and cleave sucrose for the synthesis of UDP-glucose. Since the S(11)E mutant enzyme showed the lowest Km (sucrose) and the highest catalytic efficiency of the recombinant proteins, the enzymic properties of this S11E mutant were further characterized. The results showed that replacement of Ser(11) with Glu(11) modestly protected the sucrose synthesis activity against phenolic glycosides and altered the enzyme nucleotide specificity. We postulate that the introduction of negative charge at Ser(11) is possibly involved in the enzymatic perturbation of sucrose synthase
Editor: Oxford: Oxford University Press
Idioma: Inglês

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An increase in apparent affinity for sucrose of mung bean [Vigna radiata] sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11

Nakai, T. (Kyoto Univ., Uji (Japan). Wood Research Inst.) ; Konishi, T ; Zhang, X.Q ; Chollet, R ; Tonouchi, N ; Tsuchida, T ; Yoshinaga, F ; Mori, H ; Sakai, F ; Hayashi, T

Oxford: Oxford University Press

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