Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.5.2 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)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
Homo sapiens GDP + phosphate
-
ir
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

Synonyms Comment Organism
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