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Literature summary extracted from

  • Vitale, N.; Moss, J.; Vaughan, M.
    Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1) (1998), J. Biol. Chem., 273, 2553-2560.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.5.2 expression in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.6.5.2 additional information identification of an N-terminal GAP domain Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.5.2 GTP + H2O Homo sapiens
-
 GDP + phosphate
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.2 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.5.2 recombinant enzymes, affinity chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.5.2 GTP + H2O
-
 Homo sapiens GDP + phosphate
-
 ir
3.6.5.2 guanosine 5'-O-(3-thiotriphosphate) + H2O no detectable hydrolysis of GTP at the ARF domain p3, 35-40% of the GTP bound to ARD1 domain p8 hydrolyzed in 1 h at room temperature Homo sapiens guanosine 5'-O-diphosphate + thiophosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.5.2 ARD1 ARF subfamily, stimulates cholera toxin ADP ribosyltransferase, involved in vesicular trafficking, key regulator for interaction of non-clathrin coat proteins with Golgi stacks and clathrin adaptor particles with the trans-Golgi network Homo sapiens