Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
Phosphoribosylglycinamide synthetase, N domain
Phosphoribosylglycinamide synthetase catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see Pfam:PF00289). This domain is structurally related to the PreATP-grasp domain. [1]. 2687276. Nucleotide sequence analysis of genes purH and purD involved in. the de novo purine nucleotide biosynthesis of Escherichia coli.. Aiba A, Mizobuchi K;. J Biol Chem 1989;264:21239-21246.. [2]. 9843369. X-ray crystal structure of glycinamide ribonucleotide synthetase. from Escherichia coli.. Wang W, Kappock TJ, Stubbe J, Ealick SE;. Biochemistry 1998;37:15647-15662. (from Pfam)
phosphoribosylglycinamide synthetase C domain-containing protein
Phosphoribosylglycinamide synthetase catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see Pfam:PF02787). [1]. 2687276. Nucleotide sequence analysis of genes purH and purD involved in. the de novo purine nucleotide biosynthesis of Escherichia coli.. Aiba A, Mizobuchi K;. J Biol Chem 1989;264:21239-21246.. [2]. 9843369. X-ray crystal structure of glycinamide ribonucleotide synthetase. from Escherichia coli.. Wang W, Kappock TJ, Stubbe J, Ealick SE;. Biochemistry 1998;37:15647-15662. (from Pfam)
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain
Phosphoribosylglycinamide synthetase catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see Pfam:PF02786). [1]. 2687276. Nucleotide sequence analysis of genes purH and purD involved in. the de novo purine nucleotide biosynthesis of Escherichia coli.. Aiba A, Mizobuchi K;. J Biol Chem 1989;264:21239-21246.. [2]. 9843369. X-ray crystal structure of glycinamide ribonucleotide synthetase. from Escherichia coli.. Wang W, Kappock TJ, Stubbe J, Ealick SE;. Biochemistry 1998;37:15647-15662. (from Pfam)
phosphoribosylamine--glycine ligase
phosphoribosylamine--glycine ligase catalyzes the second step of the de novo purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi
Phosphoribosylamine--glycine ligase catalyzes the formation of N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-D-ribosylamine and glycine in purine biosynthesis. It is also called glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on