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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
24
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pubmed:dateCreated |
1995-8-3
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pubmed:abstractText |
A form of phosphofructokinase (PFK) from Ascaris suum desensitized to hysteresis in the reaction time course and ATP allosteric inhibition has been used to study the activation by fructose 2,6-bisphosphate (F26P2) at varied pH in both reaction directions. In the direction of phosphorylation of F6P, V and V/KMgATP are constant over the pH range 6-9, while V/KF6P decreases at low pH, giving a pK value of 7.0, and at high pH, giving a pK of 8.9. V and V/KMgATP are insensitive to the presence of F26P2, but V/KF6P is increased by a constant amount in the presence of saturating F26P2 over the entire pH range studied. The concentration of F26P2 that gives half the change in V/KF6P, Kact, increases as the pH decreases, giving a pK of 7.4, reflecting an enzyme group that must be unprotonated for optimum binding of F26P2. In the direction of phosphorylation of MgADP, V and V/KMgADP are pH-independent, and both are insensitive to the presence of F26P2. V/KFBP decreases at high pH, giving a pK of about 7.3, and is increased by a constant amount in the presence of F26P2 over the entire pH range studied.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Fructosediphosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Fructosephosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphofructokinase-1,
http://linkedlifedata.com/resource/pubmed/chemical/fructose 2,6-diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/fructose-6-phosphate
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7781-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7794888-Adenosine Diphosphate,
pubmed-meshheading:7794888-Allosteric Regulation,
pubmed-meshheading:7794888-Animals,
pubmed-meshheading:7794888-Ascaris suum,
pubmed-meshheading:7794888-Catalysis,
pubmed-meshheading:7794888-Fructosediphosphates,
pubmed-meshheading:7794888-Fructosephosphates,
pubmed-meshheading:7794888-Hydrogen-Ion Concentration,
pubmed-meshheading:7794888-Kinetics,
pubmed-meshheading:7794888-Models, Chemical,
pubmed-meshheading:7794888-Phosphofructokinase-1,
pubmed-meshheading:7794888-Phosphorylation
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pubmed:year |
1995
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pubmed:articleTitle |
Acid-base catalytic mechanism and pH dependence of fructose 2,6-bisphosphate activation of the Ascaris suum phosphofructokinase.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of North Texas Health Science Center at Fort Worth 76107-2699, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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