Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3.

Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. Research Abstract Details 

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Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. Abstract Text:

Haiyan Chu,Philip S Low,

Previous work has shown that GAPDH (glyceraldehyde-3-phosphate dehydrogenase), aldolase, PFK (phosphofructokinase), PK (pyruvate kinase) and LDH (lactate dehydrogenase) assemble into a GE (glycolytic enzyme) complex on the inner surface of the human erythrocyte membrane. In an effort to define the molecular architecture of this complex, we have undertaken to localize the binding sites of these enzymes more accurately. We report that: (i) a major aldolase-binding site on the erythrocyte membrane is located within N-terminal residues 1-23 of band 3 and that both consensus sequences D6DYED10 and E19EYED23 are necessary to form a single enzyme-binding site; (ii) GAPDH has two tandem binding sites on band 3, located in residues 1-11 and residues 12-23 respectively; (iii) a PFK-binding site resides between residues 12 and 23 of band 3; (iv) no GEs bind to the third consensus sequence (residues D902EYDE906) at the C-terminus of band 3; and (v) the LDH- and PK-binding sites on the erythrocyte membrane do not reside on band 3. Taken together, these results argue that band 3 provides a nucleation site for the GE complex on the human erythrocyte membrane and that other components near band 3 must also participate in organizing the enzyme complex.

Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. Publishing Authors By Initials

H Chu,PS Low,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research

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Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Biochemical journal

VOLUME: 400

Page Numbers: 143-51

Journal Abbreviation: Biochem. J.

ISSN: 1470-8728

DAY: 15

MONTH: Nov

YEAR: 2006

Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2984726

Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. Keywords Mesh Terms:

KEYWORDS: Sequence Homology, Amino Acid

MESH TERMS: metabolism

Chemical & Substance for Abstract: Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. Information

Substance Name: Fructose-Bisphosphate Aldolase

Registry Number: EC 4.1.2.13

Grant and Affiliation Information for Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3.

AFFILIATION: Chemistry Department, Purdue University, 560 Oval Drive, West Lafayette, IN 47907, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM 24417

ACRONYM: GM

MEDLINETA: Biochem J

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