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

BRENDA support

Literature summary for 2.7.7.B4 extracted from

  • Schmitz, J.; Chowdhury, M.M.; Hänzelmann, P.; Nimtz, M.; Lee, E.Y.; Schindelin, H.; Leimkühler, S.
    The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins (2008), Biochemistry, 47, 6479-6489.
    View publication on PubMed
Search for more literature for 2.7.7.B4

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Urm1p-terminal-Gly-AMP + Uba4-SSH Saccharomyces cerevisiae the N-terminal domain of Uba4 catalyzes the activation of Urm1 by formation of an acyl-adenylate bond. After adenylation, persulfurated Uba4 is able to form a thiocarboxylate group at the C-terminal glycine of Urm1. The formation of a thioester intermediate between Uba4 and Urm1 is not observed. The functional similarities between Uba4 and MOCS3 (protein essential for the biosynthesis of the molybdenum cofactor in human) further demonstrate the evolutionary link between ATP-dependent protein conjugation and ATP-dependent cofactor sulfuration Urm1p-terminal-Gly-COSH + human MOCS2A-SH + AMP
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P38820
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of Uba and copurification of stable heterotetrameric complexes of Uba4 with both human Urm1 and MOCS2A Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + human MOCS2A-terminal-Gly the N-terminal domain of Uba4 catalyzes the activation of either MOCS2A (protein essential for the biosynthesis of the molybdenum cofactor in human) or Urm1 by formation of an acyl-adenylate bond. After adenylation, persulfurated Uba4 is able to form a thiocarboxylate group at the C-terminal glycine of either Urm1 or MOCS2A. The formation of a thioester intermediate between Uba4 and Urm1 or MOCS2A is not observed. The functional similarities between Uba4 and MOCS3 further demonstrate the evolutionary link between ATP-dependent protein conjugation and ATP-dependent cofactor sulfuration Saccharomyces cerevisiae diphosphate + Urm1p-terminal-Gly-AMP
-
 ?
ATP + Urm1p-terminal-Gly the N-terminal domain of Uba4 catalyzes the activation of Urm1 by formation of an acyl-adenylate bond. After adenylation, persulfurated Uba4 is able to form a thiocarboxylate group at the C-terminal glycine of Urm1 Saccharomyces cerevisiae diphosphate + Urm1p-terminal-Gly-AMP
-
 ?
Urm1p-terminal-Gly-AMP + Uba4-SSH the N-terminal domain of Uba4 catalyzes the activation of Urm1 by formation of an acyl-adenylate bond. After adenylation, persulfurated Uba4 is able to form a thiocarboxylate group at the C-terminal glycine of Urm1. The formation of a thioester intermediate between Uba4 and Urm1 is not observed. The functional similarities between Uba4 and MOCS3 (protein essential for the biosynthesis of the molybdenum cofactor in human) further demonstrate the evolutionary link between ATP-dependent protein conjugation and ATP-dependent cofactor sulfuration Saccharomyces cerevisiae Urm1p-terminal-Gly-COSH + human MOCS2A-SH + AMP
-
 ?

Synonyms

Synonyms Comment Organism
N-terminal domain of Uba4
-
 Saccharomyces cerevisiae
Uba4
-
 Saccharomyces cerevisiae