References
- Buchanan BB (1980) Role of light in the regulation of chloroplast enzymes. Annu Rev Plant Physiol 31, 341-374 https://doi.org/10.1146/annurev.pp.31.060180.002013
- 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 https://doi.org/10.1007/BF00015056
- 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 https://doi.org/10.1104/pp.75.3.561
- 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 https://doi.org/10.1016/0378-1119(89)90358-2
- 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 https://doi.org/10.1016/S1046-5928(02)00654-X
- 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 https://doi.org/10.1021/bi00232a007
-
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 https://doi.org/10.1016/S0167-4838(01)00218-7
- Kelly GJ, Zimmermann G, and Latzko E (1982) Fructosebisphosphatase from spinach leaf chloroplast and cytoplasm. Methods Enzymol 90, 371-378 https://doi.org/10.1016/S0076-6879(82)90158-6
- 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 https://doi.org/10.1016/0020-711X(92)90201-B
- Nielsen TH, Rung JH, and Villadsen D (2004) Fructose-2,6- bisphosphate: a traffic signal in plant metabolism. Trends Plant Sci 9, 556-563 https://doi.org/10.1016/j.tplants.2004.09.004
- 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 https://doi.org/10.1104/pp.100.1.210
- 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 https://doi.org/10.1074/jbc.271.6.3005
- Stitt M (1990) Fructose-2,6-bisphosphate as a regulatory molecules in plants. Annu Rev Plant Mol Biol 41, 153- 185 https://doi.org/10.1146/annurev.pp.41.060190.001101
- 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 https://doi.org/10.1104/pp.79.3.590
- 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 https://doi.org/10.1046/j.1365-313x.2000.00847.x
- 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 https://doi.org/10.1046/j.1365-313X.1996.9050671.x