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Roles of the Residues Lys115 and Tyr116 in the Binding of an Allosteric Inhibitor AMP to Pea Cytosolic Fructose-1,6-bisphosphatase
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 Title & Authors
Roles of the Residues Lys115 and Tyr116 in the Binding of an Allosteric Inhibitor AMP to Pea Cytosolic Fructose-1,6-bisphosphatase
Jang, Hye-Kyung; Cho, Man-Ho; Kwon, Yong-Kook; Bhoo, Seong-Hee; Jeon, Jong-Seong; Hahn, Tae-Ryong;
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Cytosolic fructose-1,6-bisphosphatase (cFBPase) in plants is a key regulatory enzyme in the photosynthetic sucrose biosynthesis. Plant cFBPases, like the mammalian FBPases, are inhibited by adenosine 5'-monophosphate (AMP) and fructose-2,6-bisphosphate (Fru-2,6-). In the mammalian FBPases, Lys112 and Tyr113 play important roles in the AMP binding. To understand roles of the corresponding residues, Lys115 and Tyr116, in pea cFBPase, the mutant cFBPases were generated by site-directed mutagenesis. The alterations of Lys115 to Gin and Tyr116 to Phe displayed small changes in and for Fru-2,6-, indicating that the mutation causes minor effects on the enzyme catalysis and Fru-2,6- binding, whereas resulted in higher than 500-fold increase of compared with that of the wild-type enzyme. Results indicate the residues Lys115 and Tyr116 play important roles in the binding of AMP to the allosteric site of the pea cFBPase.
adenosine 5'-monophosphate inhibition;cytosolic fructose-1,6-bisphosphatase;site-directed mutagenesis;sucrose biosynthesis;
 Cited by
Buchanan BB (1980) Role of light in the regulation of chloroplast enzymes. Annu Rev Plant Physiol 31, 341-374 crossref(new window)

Chen M, Chen L, and Fromm HJ (1994) Replacement of glutamic acid 29 with glutamine leads to a loss of cooperativity for AMP with porcine fructose-1,6-bisphosphatase. J Biol Chem 269, 5554-5558

Cho MH and Hahn TR (1991) Biochemical characteristics of the purified pea chloroplast fructose-1,6-bisphosphatase. Korean Biochem J 24, 617-624

Daie J (1993) Cytosolic fructose-1,6-bisphosphatase: A key enzyme in the sucrose biosynthetic pathway. Photosynth Res 38, 5-14 crossref(new window)

Gidh-Jain M, Zhang Y, van Poelje PD, Liang JY, Huang S, Kim J, Elliott JT, Erion MD, Pilkis SJ, El-Maghrabi MR, and Lipscomb WN (1994) The allosteric site of human liver fructose-1,6-bisphosphatase; Analysis of six AMP site mutants based on the crystal structure. J Biol Chem 269, 27732-27738

Herzog B, Stitt M, and Heldt HW (1984) Control of Photosynthetic sucrose synthesis by fructose-2,6-bisphosphate; III. Properties of the cytosolic fructose-1,6-bisphosphatase. Plant Physiol 75, 561-565 crossref(new window)

Ho SN, Hunt HD, Horton RM, Pullen JK, and Pease LR (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 crossref(new window)

Jang HK, Lee SW, Lee YH, and Hahn TR (2003) Purification and characterization of a recombinant pea cytoplasmic fructose-1,6-bisphosphatase. Protein Expr Purif 28, 42-48 crossref(new window)

Ke H, Liang JY, Zhang Y, and Lipscomb WN (1991) Conformational Transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form). Biochemistry 30, 4412-4420 crossref(new window)

Ke H, Thorpe CM, Seaton BA, Marcus F, and Lipscomb WN (1989) Molecular structure of fructose-1,6-bisphosphatase at $2.8-\AA$ resolution. Proc Natl Acad Sci USA 86, 1475-1479

Ke H, Zhang Y, and Lipscomb WN (1990) Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium. Proc Natl Acad Sci USA 87, 5243-5247

Kelly-Loughnane N and Kantrowitz ER (2001) AMP inhibition of pig kidney fructose-1,6-bisphosphatase. Biochim Biophys Acta 1548, 66-71 crossref(new window)

Kelly GJ, Zimmermann G, and Latzko E (1982) Fructosebisphosphatase from spinach leaf chloroplast and cytoplasm. Methods Enzymol 90, 371-378 crossref(new window)

Lee SW, Cho MH, Kang HC, and Hahn TR (1994) Purification and general properties of pea cytoplasmic fructose- 1,6-bisphosphatase. Korean Biochem J 27, 538-543

Liang JY, Zhang Y, Huang S, and Lipscomb WN (1993) Allosteric transition of fructose-1,6-bisphosphatase. Proc Natl Acad Sci USA 90, 2132-2136

Nel W and Terblanche SE (1992) Plant fructose-1,6-bisphosphatases: characteristics and properties. Int J Biochem 24, 1267-1283 crossref(new window)

Nielsen TH, Rung JH, and Villadsen D (2004) Fructose-2,6- bisphosphate: a traffic signal in plant metabolism. Trends Plant Sci 9, 556-563 crossref(new window)

Pilkis SJ, El-Maghrabi MR, Pilkis J, and Claus T (1981) Inhibition of fructose-1,6-bisphosphatase by fructose 2,6- bisphosphate. J Biol Chem 256, 3619-3622

Schurmann P and Wolosiuk RA (1978) Studies on the regulatory properties of chloroplast fructose-1,6-bisphosphatase. Biochim Biophys Acta 12, 130-138

Sharkey TD, Savitch LV, Vanderveer PJ, and Micallef BJ (1992) Carbon partitioning in a Flaveria linearis mutant with reduced cytosolic fructose bisphosphatase. Plant Physiol 100, 210-215 crossref(new window)

Shyur LF, Aleshin AE, Honzatko RB, and Fromm HJ (1996) Site-directed mutagenesis of residues at subunit interfaces of porcine fructose-1,6-bisphosphatase. J Biol Chem 271, 3005-3010 crossref(new window)

Stitt M (1990) Fructose-2,6-bisphosphate as a regulatory molecules in plants. Annu Rev Plant Mol Biol 41, 153- 185 crossref(new window)

Stitt M, Herzorg B, and Heldt HW (1985) Control of photosynthetic sucrose synthesis by fructose-2,6-bisphosphate; V. Modulation of the spinach leaf cytosolic fructose-1,6- bisphosphatase activity in vitro by substrate, product, pH, magnesium, fructose-2,6-bisphosphate, adenosine monophosphate, and dihydroxyacetone phosphate. Plant Physiol 79, 590-598 crossref(new window)

Strand A, Zrenner R, Trevanion S, Stitt M, Gustafsson P, and Gardestrom P (2000) Decreased expression of two key enzymes in the sucrose biosynthesis pathway, cytosolic fructose-1,6-bisphosphatase and sucrose phosphate synthase, has remarkably different consequences for photosynthetic carbon metabolism in transgenic Arabidopsis thaliana. Plant J 23, 759-770 crossref(new window)

van Schaftingen E, and Hers HG (1981) Inhibition of fructose- 1,6-bisphosphatase by fructose 2,6-bisphosphate. Proc Natl Acad Sci USA 78, 2861-2863

Xue Y, Huang S, Liang JY, Zhang Y, and Lipscomb WN (1994) Crystal structure of fructose-1,6-bisphosphatase complexed with fructose-2,6-bisphosphate, AMP, and $Zn^{2+}$ at $2.0-\AA$ resolution: Aspects of synergism between inhibitors. Proc Natl Acad Sci USA 91, 12482-12486

Zimmermann G, Kelly GJ, and Latzko E (1976) Efficient purification and molecular properties of spinach chloroplast fructose-1,6-bisphosphatase. Eur J Biochem 15, 361-367

Zimmermann G, Kelly GJ, and Latzko E (1978) Purification and Properties of spinach leaf cytoplasmic fructose- 1,6-bisphosphatase. J Biol Chem 253, 5952-595

Zrenner R, Krause KP, Apel P, and Sonnewald U (1996) Reduction of the cytosolic fructose-1,6-bisphosphatase in transgenic potato plants limits photosynthetic sucrose biosynthesis with no impact on plant growth and tuber yield. Plant J 9, 671-681 crossref(new window)