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Literature summary extracted from

  • Kinukawa, M.; Nomura, M.; Vacquier, V.D.
    A sea urchin sperm flagellar adenylate kinase with triplicated catalytic domains (2007), J. Biol. Chem., 282, 2947-2955.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.3
-
 Strongylocentrotus purpuratus
2.7.4.3 recombinant expression of full-length enzyme and each of its three catalytic domains Strongylocentrotus purpuratus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.4.3 additional information recombinant expression of full-length enzyme and each of its three catalytic domains. No enzymic activity of a sole catalytic domain Strongylocentrotus purpuratus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.3 Ca2+ 51% inhibition at 1 mM Strongylocentrotus purpuratus
2.7.4.3 P1,P5-di(adenosine-5')pentaphosphate 50% inhibition at 0.00041 mM, reactivation by 1 mM ADP if concentration of inhibitor is below 0.001 mM. No inhibition if 1 mM ADP is present; 50% inhibition at 0.00053 mM, recombinant enzyme; completely inhibits reactivation of flagella. 1 mM ADP prevents inhibition Strongylocentrotus purpuratus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.3 0.23
-
 ADP pH 7.6, 16°C, recombinant enzyme Strongylocentrotus purpuratus
2.7.4.3 0.32
-
 ADP pH 7.6, 16°C, enzyme from sperm flagellum Strongylocentrotus purpuratus
2.7.4.3 0.32
-
 ADP pH 7.6, isolated flagella Strongylocentrotus purpuratus
2.7.4.3 0.32
-
 ADP pH 7.6, 16°C Strongylocentrotus purpuratus
2.7.4.3 0.69
-
 ADP pH 7.6, 16°C, enzyme from embryonic cilia Strongylocentrotus purpuratus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.4.3 flagellum localizes along the entire flagellum, tightly bound to the axoneme. Enzyme contributes 31% of the total non-mitochondrial ATP synthesis associated with the demembranated axoneme Strongylocentrotus purpuratus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.4.3 130000
-
 x * 130000, full-length enzyme, 21000, recombinant expression of catalytic domain 1 or 3, 22000, recombinant expression of catalytic domain 2, SDS-PAGE Strongylocentrotus purpuratus

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.3 Strongylocentrotus purpuratus
-
-
-
2.7.4.3 Strongylocentrotus purpuratus A2T1M5
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.4.3 phosphoprotein n vitro phosphorylation results in 19% increase of vmax Strongylocentrotus purpuratus

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.7.4.3 reactivation of enzyme inhibited by P1,P5-di(adenosine-5’)-pentaphosphate with 1 mM ADP if concentration of inhibitior is below 0.001 mM Strongylocentrotus purpuratus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.4.3 embryo embryonic cilia Strongylocentrotus purpuratus
-
2.7.4.3 flagellate most of protein is tightly bound to the axoneme Strongylocentrotus purpuratus
-
2.7.4.3 sperm flagellum
-
 Strongylocentrotus purpuratus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.3 ADP
-
 Strongylocentrotus purpuratus ATP + AMP
-
 ?
2.7.4.3 ADP
-
 Strongylocentrotus purpuratus ATP + AMP
-
 r
2.7.4.3 ADP
-
 Strongylocentrotus purpuratus AMP + ATP
-
 ?
2.7.4.3 ATP + AMP
-
 Strongylocentrotus purpuratus 2 ADP
-
 r
2.7.4.3 additional information at the measured in vivo concentrations of ADP of 0.114 mM, at pH 7.6, the axonemal adenylate kinase could contribute31%, and creatine kinase 69%, of the total non-mitochondrial ATP synthesis associated with the demembranated axoneme. The three catalytic domains of adenylate kinase are considerably divergent from each other Strongylocentrotus purpuratus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.4.3 ? x * 130000, full-length enzyme, 21000, recombinant expression of catalytic domain 1 or 3, 22000, recombinant expression of catalytic domain 2, SDS-PAGE Strongylocentrotus purpuratus
2.7.4.3 More enzyme has three catalytic domains Strongylocentrotus purpuratus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.3 7.7
-
-
 Strongylocentrotus purpuratus
2.7.4.3 8.1
-
 recombinant enzyme Strongylocentrotus purpuratus

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.4.3 0.00041
-
 pH 7.6, 16°C Strongylocentrotus purpuratus P1,P5-di(adenosine-5')pentaphosphate