Results 221 to 230 of about 11,445 (270)

Mechanistic and applied study of phosphofructokinases, the "gatekeeper" of the glycolytic pathway on the central carbon metabolism. [PDF]

Metab Eng Commun
Li L, Chen X, Zhang Y, Qin N, Chen Y, Ji X, Nielsen J, Liu Z.   +7 more
europepmc   +1 more source

Metabolic Vulnerabilities as a Therapeutic Target in Breast Cancer. [PDF]

Curr Oncol
Guo S, Addison CL.
europepmc   +1 more source

Glycerol and Glycerol-3-Phosphate: Multifaceted Metabolites in Metabolism, Cancer, and Other Diseases. [PDF]

Endocr Rev
Madiraju SRM, Possik E, Al-Mulla F, Nolan CJ, Prentki M.   +4 more
europepmc   +1 more source

A dual L-glucose/L-galactose catabolic pathway in <i>Luteolibacter</i> species strain LG18. [PDF]

J Bacteriol
Yachida M, Shiratori Y, Iwabuchi S, Shimizu T, Nakamura A.   +4 more
europepmc   +1 more source

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Glyceraldehyde 3-phosphate dehydrogenases

Journal of Molecular Biology, 1965
Publisher Summary This chapter discusses about glyceraldehyde 3-phosphate dehydrogenase. The subunit structure of several NAD-linked dehydrogenases is now well established. Comparison of the amino-acid sequence of glyceraldehyde 3-phosphate dehydrogenases from different species is of interest from the point of view of three-dimensional structure and ...
J. Ieuan Harris, R.N. Perham
openaire   +3 more sources

Acyl Derivatives of Glyceraldehyde-3-Phosphate Dehydrogenase

Science, 1955
Acetyl phosphate and 1,3-diphosphoglycerate react with glyceraldehyde-3-phosphate dehydrogenase to form relatively stable enzyme substrate compounds. These compounds appear to be thiol esters, and their properties indicate that they are intermediates in the catalytic activity of the enzyme: they undergo hydrolysis and arsenolysis in the presence of DPN
I, KRIMSKY, E, RACKER
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Inactivation of glyceraldehyde 3-phosphate dehydrogenase

Archives of Biochemistry and Biophysics, 1967
Abstract Enzymatic activity and physical chemical properties have been determined for yeast glyceraldehyde 3-phosphate dehydrogenase (GPD) exposed to low and high pH. Inactivation of the enzyme is rapid below pH 4.5 and above pH 11, and is accompanied by a decrease in sedimentation constant resulting in large part from dissociation into its ...
Y, Shibata, M J, Kronman
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Glyceraldehyde-3-phosphate dehydrogenase and apoptosis

Journal of Neuroscience Research, 2000
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as playing an integral role in glycolysis. During the past 20 years, however, a number of novel, additional functions for GAPDH have been described. These include acting as an uracil DNA glycosylase, activator of transcription, binding to RNA, and an involvement in tubulin ...
M D, Berry, A A, Boulton
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Hybridization of Glyceraldehyde-3-phosphate Dehydrogenase

The Journal of Biochemistry, 1975
1. Glyceraldehyde-3-phosphate dehydrogenases [EC 1.2.1.12] from rabbit, pig, lobster, yeast, E. coli, and B. stearothermophilus have been subjected to hybridization in 3M NaCL. 2. Suitable mixtures of electrophoretically distinct glyceraldehyde-3-phosphate dehydrogenases were found to give five-membered by electrophoresis on cellulose acetate. 3.
K, Suzuki, J I, Harris
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Molecular Symmetry of Glyceraldehyde-3-phosphate Dehydrogenase

Journal of Molecular Biology, 1972
Abstract The rotation function has been used to determine the orientation of the molecule of lobster glyceraldehyde- 3-phosphate dehydrogenase in its crystal cell. The results have also established the 222 symmetry of the molecule. Comparison with the known structure of lactate dehydrogenase suggests structural similarities and indicates the relative
M G, Rossmann, G C, Ford, H C, Watson, L J, Banaszak   +3 more
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