Results 201 to 210 of about 21,838 (240)

Fructose-bisphosphate aldolases: an evolutionary history

Trends in Biochemical Sciences, 1992
Two mechanistically distinct forms of fructose-bisphosphate aldolase are known to exist. It has been assumed that the Class II (metallo) aldolases are evolutionary more primitive than their Class I (Schiff-base) analogs since the latter had only been found in eukaryotes.
J J, Marsh, H G, Lebherz
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Phosphorylation of fructose bisphosphate aldolase in Trypanosoma brucei

Molecular and Biochemical Parasitology, 1989
Methods were developed for in vivo labelling of trypanosome proteins with inorganic phosphate and the labelling of fructose bisphosphate aldolase and variant surface glycoprotein was investigated. It was found that the large pool size of phosphate in trypanosomes precludes detailed kinetic analyses. Aldolase contains low levels of phosphoserine but the
C E, Clayton, J A, Fox
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Continuous colorimetric monitoring of the fructose bisphosphate aldolase reaction

Analytical Biochemistry, 1980
A simple method for continuous spectrophotometric assay of fructose-1,6-bisphosphate aldolase is described. The method is based on the reactivity of the product triose phosphates with cyanide to form compounds capable of the reduction of cytochrome c. At the concentrations employed, cyanide, acting catalytically, reacts with the enediol tautomer of the
P, Robertson, I, Fridovich
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A data-based reaction mechanism for type I fructose bisphosphate aldolase

Trends in Biochemical Sciences, 1993
The structures of three type I fructose-1,6-bisphosphate aldolases have been determined and the common residues surrounding the Schiff base-forming Lys residue located. Armed with this information, it is now possible to propose a mechanism for this ubiquitous enzyme which is consistent with the recorded biochemical data. An interesting, but by no means
J A, Littlechild, H C, Watson
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Characterization of the genes for fructose-bisphosphate aldolase in Trypanosoma brucei

Molecular and Biochemical Parasitology, 1988
In Trypanosoma brucei stock 427 the glycolytic enzyme fructose-bisphosphate aldolase is encoded by two tandemly linked genes of identical sequence. Such a tandem arrangement of aldolase genes is also present in other T. brucei stocks of unrelated origin.
M, Marchand, A, Poliszczak, W C, Gibson, R K, Wierenga, F R, Opperdoes, P A, Michels   +5 more
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Acetylation of fructose-bisphosphate aldolase-mediated glycolysis is essential for Bombyx mori nucleopolyhedrovirus infection

Microbial Pathogenesis, 2022
Bombyx mori nucleopolyhedrovirus (BmNPV) is a baculovirus that infects silkworms, and its interaction with silkworm has been considered an important model in the field of insect virology. Accumulating evidence indicates that most viruses promote glycolytic metabolism in host cells to favor infection.
Xu, Gao, Siqi, Xu, Yuqian, Mo, Yajie, Zhu, Xi, Chen, Meng, Miao, Yanping, Quan, Wei, Yu   +7 more
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[37] Fructose-bisphosphate aldolases from mycobacteria

1982
Publisher Summary This chapter describes an assay method, purification, and properties of fructose-bisphosphate aldolases from mycobacteria. Fructose-bisphosphate aldolase catalyzes the reversible cleavage of fructose bisphosphate (Fru-P2) to glyceraldehydes 3-phosphate and dihydroxyacetone phosphate.
N. Jayanthi Bai, M. Ramachandra Pai, P. Suryanarayana Murthy, T.A. Venkitasubramanian   +3 more
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Fructose-bisphosphate aldolase from Helix pomatia—I. Purification and catalytic properties

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1980
Abstract 1. 1. Fructose 1,6-bisphosphate aldolase has been purified 450 fold from Helix pomatia (snail) muscle. 2. 2. The enzyme is inhibited by NaBH4 in the presence of dihydroxyacetone phosphate and is therefore a class I aldolase. 3. 3.
Janina Buczylko, Paul A. Hargrave, Marian Kochman   +2 more
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Fructose-bisphosphate aldolase from Helix pomatia—II. Chemical and physical properties

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1980
Abstract 1. 1. Fructose-bisphosphate aldolase from Helix pomatia is a tetramer of 40,000 mol. wt. sub-units like mammalian aldolases. 2. 2. The snail enzyme differs slightly in amino acid composition from mammalian aldolases and has glycine as its amino terminus rather than proline. 3. 3.
Janina Buczylko, Paul A. Hargrave, Marian Kochman   +2 more
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