Literature summary for 2.4.2.8 extracted from

Sauve, A.A.; Cahill, S.M.; Zech, S.G.; Basso, L.A.; Lewandowicz, A.; Santos, D.S.; Grubmeyer, C.; Evans, G.B.; Furneaux, R.H.; Tyler, P.C.; McDermott, A.; Girvin, M.E.; Schramm, V.L.
Ionic States of Substrates and Transition State Analogues at the Catalytic Sites of N-Ribosyltransferases (2003), Biochemistry, 42, 5694-5705.

Search for more literature for 2.4.2.8

Cloned(Commentary)

Cloned (Comment)	Organism
functional expression in Escherichia coli	Tritrichomonas suis

Inhibitors

Inhibitors	Comment	Organism	Structure
immucillin-H	transition state analogue, binds tightly to the active site, inhibition mechanism and kinetics	Tritrichomonas suis
immucillin-H 5'-phosphate	transition state analogue, binds tightly to the active site, inhibition mechanism and kinetics	Tritrichomonas suis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Tritrichomonas suis

Organism

Organism	UniProt	Comment	Textmining
Tritrichomonas suis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant from Escherichia coli	Tritrichomonas suis

Reaction

Reaction	Comment	Organism	Reaction ID
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate	catalytic mechanism	Tritrichomonas suis	a
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate	active site structure	Tritrichomonas suis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
guanine + 5-phospho-alpha-D-ribose 1-diphosphate	-	Tritrichomonas suis	GMP + diphosphate	-	r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate	-	Tritrichomonas suis	IMP + diphosphate	-	r

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)