Literature summary for 6.3.5.3 extracted from

Morar, M.; Anand, R.; Hoskins, A.A.; Stubbe, J.; Ealick, S.E.
Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily (2006), Biochemistry, 45, 14880-14895.

Search for more literature for 6.3.5.3

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop method, enzyme in complex with formylglycinamide ribonucleotide, mutant enzyme H72A in complex with beta,gamma-methylene adenosine 5'-triphosphate, mutant enzyme H72A in complex with ADP, enzyme in complex with formylglycinamide ribonucleotide and beta,gamma-methylene adenosine 5'-triphosphate, enzyme in complex with ATP	Thermotoga maritima

Protein Variants

Protein Variants	Comment	Organism
H32A	no synthesis of formylglycinamidine ribonucleotide detected	Thermotoga maritima
H32Q	no synthesis of formylglycinamidine ribonucleotide detected	Thermotoga maritima
H72A	mutant enzyme displays 1/20 of the wild type activity with a strongly increased Km for formylglycinamidine ribonucleotide	Thermotoga maritima
H72Q	mutant enzyme displayed 1/200 of the wild type activity	Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9X0X3	-	-

Purification (Commentary)

Purification (Comment)	Organism
wild-type and mutant enzymes expression in Escherichia coli	Thermotoga maritima

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O	fourth step of the purine biosynthetic pathway	Thermotoga maritima	ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate	-	?

Synonyms

Synonyms	Comment	Organism
FGAR-AT	-	Thermotoga maritima
TmPurL	-	Thermotoga maritima

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)