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Literature summary for 2.1.2.3 extracted from

  • Wang, Y.; Mitchell-Ryan, S.; Raghavan, S.; George, C.; Orr, S.; Hou, Z.; Matherly, L.H.; Gangjee, A.
    Novel 5-substituted pyrrolo[2,3-d]pyrimidines as dual inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase and as potential antitumor agents (2015), J. Med. Chem., 58, 1479-1493.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis of human enzyme complexed with the sulfamido-bridged N-[(S)-(4-([(2-amino-4-hydroxy-quinazolin-6-yl)dihydroxy-lambda-4-sulfanyl]amino)phenyl)-hydroxymethyl]-L-glutamic acid at 2.55 A resolution, PDB ID 1P4R Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
(S)-2-(5-(3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)propyl)thiophene-2-carboxamido)pentanedioic acid inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase Homo sapiens
(S)-2-(5-(4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)butyl)thiophene-2-carboxamido)pentanedioic acid inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase Homo sapiens
additional information design and synthesis of a series of 5-substituted thiopheneyl pyrrolo[2,3-d]pyrimidines with varying chain lengths (n = 1-6). The compounds show dual inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, analysis of the unique structure-activity relationship for transport and dual target inhibition, molecular modeling and computational studies using crystal structure of human AICARFTase at 2.55 A resolution, PDB ID 1P4R, overview. No inhibition by N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid, N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid, N-([5-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]thiophen-2-yl]carbonyl)-L-glutamic acid, N-([5-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophen-2-yl]carbonyl)-L-glutamic acid, and (S)-2-(5-(5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)pentyl)thiophene-2-carboxamido)pentanedioic acid Homo sapiens
N-[(S)-(4-([(2-amino-4-hydroxy-quinazolin-6-yl)dihydroxy-lambda-4-sulfanyl]amino)phenyl)-hydroxymethyl]-L-glutamic acid binding structure, docking study and crystal structure analysis Homo sapiens
N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase Homo sapiens
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase Homo sapiens
pemetrexed the enzyme is a pharmacologically important target of anticancer drug pemetrexed, an antifolate inhibitor Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P31939
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Source Tissue

Source Tissue Comment Organism Textmining
KB cell
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Homo sapiens
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Synonyms

Synonyms Comment Organism
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
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Homo sapiens
AICA ribonucleotide formyltransferase
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Homo sapiens
AICARFTase
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Homo sapiens
ZMP formyltransferase
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Homo sapiens

General Information

General Information Comment Organism
malfunction inhibition of the enzyme results in depletion of purine nucleotides Homo sapiens
physiological function the enzyme is involved in purine nucleotide biosynthesis Homo sapiens