Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase

Proteins: Structure, Function and Genetics

Volumn 72, Issue 1, 2008, Pages 209-216

  Gizak, Agnieszka ^a   Maciaszczyk, Ewa ^a   Dzugaj, Andrzej ^a   Eschrich, Klaus ^b   Rakus, Darek ^a  

^a UNIVERSITY OF WROC AW   (Poland)

^b UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

FBPase; Muscle glyconeogenesis; N terminus; Protein protein interaction; Subcellular localization

Indexed keywords

ADENOSINE PHOSPHATE; CALCIUM; FRUCTOSE BISPHOSPHATASE; FRUCTOSE BISPHOSPHATE ALDOLASE; MAGNESIUM;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DESENSITIZATION; ENERGY EXPENDITURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INHIBITION; ENZYME KINETICS; ENZYME REGULATION; HUMAN; METABOLITE; MOLECULAR EVOLUTION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN INTERACTION;

AMINO ACID SEQUENCE; CALCIUM; CONSERVED SEQUENCE; EVOLUTION, MOLECULAR; FRUCTOSE-BISPHOSPHATASE; FRUCTOSE-BISPHOSPHATE ALDOLASE; HUMANS; KINETICS; MAGNESIUM; MOLECULAR SEQUENCE DATA; MUSCLES; MUTANT PROTEINS; PROTEIN BINDING; RHODAMINES; SARCOMERES; STRUCTURE-ACTIVITY RELATIONSHIP;

VERTEBRATA;

EID: 44949168573     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21909     Document Type: Article

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