Results 161 to 170 of about 10,894 (204)

Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase

Nature, 2011
Enzymes catalyse specific reactions and are essential for maintaining life. Although some are referred to as being bifunctional, they consist of either two distinct catalytic domains or a single domain that displays promiscuous substrate specificity. Thus, one enzyme active site is generally responsible for one biochemical reaction. In contrast to this
Shinya, Fushinobu, Hiroshi, Nishimasu, Daiki, Hattori, Hyun-Jin, Song, Takayoshi, Wakagi   +4 more
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Suicide inactivation of fructose 1,6-bisphosphate aldolase

Biochemistry, 1984
2-Keto-4,4,4-trifluorobutyl phosphate (HTFP) was prepared from 3,3,3-trifluoropropionic acid. HTFP acts as an irreversible inhibitor of rabbit muscle aldolase: the loss of activity was time dependent and the inactivation followed a pseudo-first-order process.
A, Magnien, B, Le Clef, J F, Biellmann
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Fructose 1,6-bisphosphate aldolase activity ofRhizobium species

Folia Microbiologica, 1975
FDP aldolase was found to be present in the cell-free extracts of Rhizobium leguminosarum, Rhizobium phaseoli, Rhizobium trifolii, Rhizobium meliloti, Rhizobium lupini, Rhizobium japonicum and Rhizobium species from Arachis hypogaea and Sesbania cannabina. The enzyme in 3 representative species has optimal activity at pH 8.4 in 0.2M veronal buffer. The
K A, Siddiqui, A K, Banerjee
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Molecular Evolution of Amphioxus Fructose-1,6- bisphosphate Aldolase

Archives of Biochemistry and Biophysics, 1997
The cDNA for amphioxus fructose-1,6-bisphosphate (FBP)-aldolase was isolated and its nucleotide sequence was determined. In the cDNA, there existed a probable open reading frame comprising 1080 bp; hence, 359 amino acid residues were deduced. The amino acid sequence indicates the deletion of 4 residues from N-terminus, in comparison with the sequence ...
M, Kuba, H, Yatsuki, T, Kusakabe, Y, Takasaki, N, Nikoh, T, Miyata, T, Yamaguchi, K, Hori   +7 more
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The structure of human liver fructose-1,6-bisphosphate aldolase

Acta Crystallographica Section D Biological Crystallography, 2001
The X-ray crystallographic structure of the human liver isozyme of fructose-1,6-bisphosphate aldolase has been determined by molecular replacement using a tetramer of the human muscle isozyme as a search model. The liver aldolase (B isozyme) crystallized in space group C2, with unit-cell parameters a = 291.1, b = 489.8, c = 103.4 A, alpha = 90, beta ...
A R, Dalby, D R, Tolan, J A, Littlechild
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Fructose 1,6-Bisphosphate Aldolase Is a Heparin-Binding Protein

Journal of Biochemistry, 1999
Proteins with affinity to heparin under physiological conditions were isolated from bovine cerebral cortex. First, the extract of cerebral cortex was applied to a chondroitin polysulfate column under physiological conditions. Then, the pass-through fraction was applied to a heparin column.
T V, Ta, R, Takano, K, Kamei, X Y, Xu, Y, Kariya, K, Yoshida, S, Hara   +6 more
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Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus

Biochemical and Biophysical Research Communications, 2006
It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively.
Jun Hyuck, Lee, Jungdon, Bae, Dooil, Kim, Yongseok, Choi, Young Jun, Im, Sukhoon, Koh, Joong Su, Kim, Mun-Kyoung, Kim, Gil Bu, Kang, Suk-In, Hong, Dae-Sil, Lee, Soo Hyun, Eom   +11 more
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Characterization and localization of Opisthorchis viverrini fructose-1,6-bisphosphate aldolase

Parasitology International, 2017
Opisthorchis viverrini (Ov) infection is a long-time public health problem in Thailand that can lead to bile duct cancer, cholangiocarcinoma (CCA). Characterization of the Ov proteins at a molecular level will increase our knowledge of host-parasite interaction that can be applied to new drug, vaccine, or immunodiagnostic development. In this study, an
Jeerati, Prompipak, Thanaset, Senawong, Khuanta, Jokchaiyaphum, Kornpira, Siriwes, Suporn, Nuchadomrong, Thewarach, Laha, Banchob, Sripa, Gulsiri, Senawong   +7 more
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Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase

Nature Structural & Molecular Biology, 1996
The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit.
N S, Blom, S, Tétreault, R, Coulombe, J, Sygusch   +3 more
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Phosphate modification of fructose-1,6-bisphosphate aldolase in Escherichia coli

Biochemical and Biophysical Research Communications, 1988
When E. coli carrying multicopy plasmids for fructose-1,6-P2 aldolase or phosphoglycerate kinase was grown in the presence of 32Pi, there was label at the position of cognate high level polypeptide after SDS-PAGE. As tested for aldolase, the label was resistant to acetone, RNase, and hot TCA treatments, and was also observed by immunoprecipitation ...
J, Babul, D G, Fraenkel
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