Zobrazeno 1 - 10
of 203
pro vyhledávání: '"Herbert J. Fromm"'
Publikováno v:
Journal of Biological Chemistry. 284:20240-20248
The PduX enzyme of Salmonella enterica is an l-threonine kinase used for the de novo synthesis of coenzyme B(12) and the assimilation of cobyric acid. PduX with an N-terminal histidine tag (His(8)-PduX) was produced in Escherichiacoli and purified. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5691dadf0ad15ba31dbd2f896a368ccd
https://doi.org/10.1074/jbc.m109.027425
https://doi.org/10.1074/jbc.m109.027425
Publikováno v:
Journal of Biological Chemistry. 282:36121-36131
Fructose-1,6-bisphosphatase (FBPase) operates at a control point in mammalian gluconeogenesis, being inhibited synergistically by fructose 2,6-bisphosphate (Fru-2,6-P(2)) and AMP. AMP and Fru-2,6-P(2) bind to allosteric and active sites, respectively
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeec1328ad521db2b435a2002a49be60
https://doi.org/10.1074/jbc.m707302200
https://doi.org/10.1074/jbc.m707302200
Publikováno v:
Photochemistry and Photobiology. 74:679-685
The environment of Trp57, introduced by the mutation of a tyrosine in the dynamic loop of porcine liver fructose-1,6-bisphosphatase (FBPase), was examined using time-resolved fluorescence and directed mutation. The Trp57 enzyme was studied previously
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a136b891a6471d13bd145d9d1e93b06
https://doi.org/10.1562/0031-8655(2001)0740679eotipf2.0.co2
https://doi.org/10.1562/0031-8655(2001)0740679eotipf2.0.co2
Publikováno v:
Journal of Biological Chemistry. 282:11696-11704
The enteric bacterium Escherichia coli requires fructose-1,6-bisphosphatase (FBPase) for growth on gluconeogenic carbon sources. Constitutive expression of FBPase and fructose-6-phosphate-1-kinase coupled with the absence of futile cycling implies an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::35b92165de29713b14ac0f4f17f3d080
https://doi.org/10.1074/jbc.m611104200
https://doi.org/10.1074/jbc.m611104200
Publikováno v:
Journal of Biological Chemistry. 280:38403-38409
One molecule of glucose 6-phosphate inhibits brain hexokinase (HKI) with high affinity by binding to either one of two sites located in distinct halves of the enzyme. In addition to potent inhibition, glucose 6-phosphate releases HKI from the outer l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48ff8fc7351a573eec5f6d9556e1a140
https://doi.org/10.1074/jbc.m506943200
https://doi.org/10.1074/jbc.m506943200
Publikováno v:
Journal of Biological Chemistry. 279:18481-18487
Fructose-1,6-bisphosphatase requires a divalent metal cation for catalysis, Mg(2+) being its most studied activator. Phosphatase activity increases sigmoidally with the concentration of Mg(2+), but the mechanistic basis for such cooperativity is unkn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d31b13904b3a1e5b9254558dab1ce4f
https://doi.org/10.1074/jbc.m308811200
https://doi.org/10.1074/jbc.m308811200
Autor:
William Charles Ripka, Scott W. Nelson, Kevin M. Short, Michael J. Newman, Richard B. Honzatko, Karl Norvell, Frank U. Axe, Kristen L. Arienti, Deborah H. Slee, Tassie L. Collins, Todd K. Jones, Jun-young Choe, Herbert J. Fromm, Rachel Denise Anne Kimmich, Suzanne J. Romano
Publikováno v:
Journal of Biological Chemistry. 278:51176-51183
A highly constrained pseudo-tetrapeptide (OC252-324) further defines a new allosteric binding site located near the center of fructose-1,6-bisphosphatase. In a crystal structure, pairs of inhibitory molecules bind to opposite faces of the enzyme tetr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ea24c33701eda690081ee60805f1970
https://doi.org/10.1074/jbc.m308396200
https://doi.org/10.1074/jbc.m308396200
Publikováno v:
Journal of Biological Chemistry. 278:16015-16020
The hydrolysis of a phosphate ester can proceed through an intermediate of metaphosphate (dissociative mechanism) or through a trigonal bipryamidal transition state (associative mechanism). Model systems in solution support the dissociative pathway,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ea0003fef8c0cd11583a15e67558902
https://doi.org/10.1074/jbc.m212395200
https://doi.org/10.1074/jbc.m212395200
Publikováno v:
Journal of Biological Chemistry. 278:6673-6679
Vertebrates have acidic and basic isozymes of adenylosuccinate synthetase, which participate in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle. These isozymes differ in their kinetic properties and N-leader se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f61b1782c5075301d81ed452046ff1fa
https://doi.org/10.1074/jbc.m210838200
https://doi.org/10.1074/jbc.m210838200
Autor:
Richard B. Honzatko, Zhenglin Hou, Wenyan Wang, Herbert J. Fromm, Eric S. Underbakke, Andrea Gorrell
Publikováno v:
Journal of Biological Chemistry. 277:8817-8821
Adenylosuccinate synthetase governs the first committed step in the de novo synthesis of AMP. Mutations of conserved residues in the synthetase from Escherichia coli reveal significant roles for Val(273) and Thr(300) in the recognition of l-aspartate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19e383fa7f346dba99f8eed4f0bd0480
https://doi.org/10.1074/jbc.m111810200
https://doi.org/10.1074/jbc.m111810200