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Nucleotide-binding sites on Escherichia coli F1-ATPase. Specificity of noncatalytic sites and inhibition at catalytic sites by MgADP

Autor: Y M Milgrom, E A Bramhall, Richard L. Cross, D J Hyndman

Publikováno v: Journal of Biological Chemistry. 269:28871-28877

Nucleotide-depleted EcF1 binds a maximum of two GTP, ATP, or ADP at noncatalytic sites, whereas all three sites can only be filled by a combination of nucleoside di- and triphosphates. MgPPi prevents binding of GTP and significantly slows ATP binding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::50a042400864717a23137bea79164a9b
https://doi.org/10.1016/s0021-9258(19)61988-5

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Nucleotide-binding sites on Escherichia coli F1-ATPase. Specificity of noncatalytic sites and inhibition at catalytic sites by MgADP

Autor: D J, Hyndman, Y M, Milgrom, E A, Bramhall, R L, Cross

Publikováno v: The Journal of biological chemistry. 269(46)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::96fbece5c7334f2802ba4662dc9ee7d4
https://pubmed.ncbi.nlm.nih.gov/7961847

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Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding

Autor: T J, Kubiseski, D J, Hyndman, N A, Morjana, T G, Flynn

Publikováno v: The Journal of biological chemistry. 267(10)

Steady state kinetic analysis at pH 7.0 of the reduction of DL-glyceraldehyde by pig muscle aldose reductase showed that the enzyme follows a sequential ordered mechanism with NADPH binding first. However, the "off constant" for NADP+ in the forward

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9572b54a820c481a20667dc9bbeacd93
https://pubmed.ncbi.nlm.nih.gov/1551865

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