Any feedback?
No. of entries
Information on EC 2.1.2.3 - phosphoribosylaminoimidazolecarboxamide formyltransferase
for references in articles please use BRENDA:EC2.1.2.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.2 Hydroxymethyl-, formyl- and related transferases
2.1.2.3 phosphoribosylaminoimidazolecarboxamide formyltransferase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.1.2.3
-
amp-activated
- methotrexate
- glycinamide
-
folate-dependent
- antifolate
- medicine
- polyglutamates
-
faicar
- garftase
- folylpolyglutamate
-
pyrrolo2,3-dpyrimidines
- 10-formyldihydrofolate
- garft
- drug development
- diagnostics
Reaction Schemes
showSynonyms
5-aminoimidazole-4-carboxamide ribonucleotide, aicar transformylase, aicar tfase, aicarft, 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, aicarft/impchase, aminoimidazolecarboxamide ribonucleotide transformylase, aica ribonucleotide formyltransferase, aminoimidazole-4-carboxamide ribonucleotide transformylase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
-
-
-
-
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
-
-
-
-
5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase
-
-
-
-
5-amino-4-imidazolecarboxamide ribonucleotide transformylase
-
-
-
-
5-amino-4-imidazolecarboxamide ribotide transformylase
-
-
-
-
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
5-aminoimidazole-4-carboxamide ribonucleotide transformylase
5-aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Tfase)-inosine monophosphate cyclohydrolase
-
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase
-
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase
5-aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase
ADE16
AICA ribonucleotide formyltransferase
AICAR formyltransferase
AICAR TFase
AICAR transformylase
AICAR transformylase/IMP cyclohydrolase
AICAR transformylase/inosine monophosphate cyclohydrolase
AICARFT
AICARFTase
aminoimidazolecarboxamide ribonucleotide transformylase
-
-
-
-
aminoimidazolecarboxamide ribotide transformylase
ATIC
Bifunctional purine biosynthesis protein
Bifunctional purine biosynthesis protein ADE16
CLasATIC
IMP: 5-aminoimidazole-4-carboxamide ribonucleotide transformylase
PurH
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
-
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
-
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
Q6IN16
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase
-
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase
-
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase
-
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase
-
-
5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase
-
-
-
5-aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase
-
bifunctional enzyme
5-aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase
bifunctional enzyme
AICAR formyltransferase
-
-
-
-
AICAR transformylase
-
-
-
-
AICAR transformylase/inosine monophosphate cyclohydrolase
-
bifunctional enzyme catalyzing the last two steps of the purine de novo synthesis pathway
AICAR transformylase/inosine monophosphate cyclohydrolase
bifunctional enzyme catalyzing the last two steps of the purine de novo synthesis pathway
AICAR transformylase/inosine monophosphate cyclohydrolase
-
bifunctional enzyme catalyzing the last two steps of the purine de novo synthesis pathway
AICAR transformylase/inosine monophosphate cyclohydrolase
bifunctional enzyme catalyzing the last two steps of the purine de novo synthesis pathway
ATIC
-
bifunational enzyme with AICAR-transformylase and IMP cyclohydrolase activities
ATIC
-
bifunctional enzyme showing 5-aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase activities
ATIC
-
bifunctional enzyme with aminoimidazolecarboxamide ribonucleotide formyl transferase and inosine monophosphate cyclohydrolase activities
ATIC
bifunctional enzyme showing 5-aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase activities
ATIC
bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase activities
ATIC
-
bifunctional enzyme showing 5-aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase activities
IMP: 5-aminoimidazole-4-carboxamide ribonucleotide transformylase
-
IMP: 5-aminoimidazole-4-carboxamide ribonucleotide transformylase
Cryptococcus neoformans ATCC 208821
-
-
IMP: 5-aminoimidazole-4-carboxamide ribonucleotide transformylase
Cryptococcus neoformans CBS 10515
-
-
IMP: 5-aminoimidazole-4-carboxamide ribonucleotide transformylase
Cryptococcus neoformans FGSC 9487
-
-
IMP: 5-aminoimidazole-4-carboxamide ribonucleotide transformylase
-
-
PurH
-
bifunctional enzyme with tranformylase and IMP cyclohydrolase activities
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
formyl group transfer
formyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
inosine-5'-phosphate biosynthesis I, inosine-5'-phosphate biosynthesis II
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carboxamide N-formyltransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9032-03-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(6R,6S)-10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
Substrates: -
Products: -
Products: -
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyl-7,8-dihydropteroylpenta-gamma-glutamate + 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide
7,8-dihydropteroylpenta-gamma-glutarate + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyl-7,8-dihydropteroylpenta-gamma-L-glutamate + 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide
dihydrofolic acid pentaglutamate + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyl-8-deazafolate + 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide
8-deazafolate + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyl-tetrahydrofolic acid + 5'-phosphoribosyl-5-amino-imidazole-carboxamide
5,6,7,8-tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyldihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyldihydrofolic acid pentaglutamate + 5-aminoimidazole-4-carboxamide
?
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-imidazole-4-thiocarboxamide ribonucleotide
tetrahydrofolate + 6-mercaptopurine ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
N10-formyltetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydropteroylheptaglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydropteroylhexaglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydropteroylmonoglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylmonoglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydropteroylpentaglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydropteroyltetraglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydropteroyltriglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydorpteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
?
N5,N10-anhydroformyltetrahydrofolic acid + glycinamide ribonucleotide
N10-formyltetrahydrofolic acid + formylglycinamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: 10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase
Products: -
Products: -
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: 10-formyl-7,8-dihydrofolate is kinetically preferred over 10-formyl-5,6,7,8-tetrahydrofolate by AICAR transformylas
Products: -
Products: -
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: 10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase
Products: -
Products: -
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: 10-formyl-7,8-dihydrofolate is kinetically preferred over 10-formyl-5,6,7,8-tetrahydrofolate by AICAR transformylas
Products: -
Products: -
r
10-formyldihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyldihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: precursors for inosinic acid biosynthesis
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: penultimate and final steps in the de novo purine biosynthesis pathway
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: de novo synthesis of purine nucleotides
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: reduced folate cofactor requiring step of de novo purine biosynthesis
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
Substrates: penultimate and final steps in the de novo purine biosynthesis pathway
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: penultimate and final steps in the de novo purine biosynthesis pathway
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: de novo synthesis of purine nucleotides
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: reduced folate cofactor requiring step of de novo purine biosynthesis
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: de novo synthesis of purine nucleotides
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans ATCC 208821
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans CBS 10515
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans FGSC 9487
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Q6IN16
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: the two activities of the bifunctional AICAR transformylase/IMP cyclohydrolase reside on separate domains
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
172161, 172163, 485742, 485745, 485746, 485747, 485748, 485749, 485750, 485753, 485755, 485757, 485758, 485759, 485760
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans ATCC 208821
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans CBS 10515
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans FGSC 9487
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: the two activities of the bifunctional AICAR transformylase/IMP cyclohydrolase reside on separate domains
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with N5,N10-methenyl analogues
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: polymorphisms in 5-aminoimidazole-4-carboxamide ribonucleotide transformylase gene is not associated with recurrent venous thrombosis risk
Products: -
Products: -
?
additional information
?
-
-
Substrates: 10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase. Bioactivity of the unnatural isomer [6R]-5-formyltetrahydrofolate is in vivo converted to 10-formyl-7,8-dihydrofolate and serves thus as a substrate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme forms a complex with its substrate via the phosphate-binding pocket of the IMP cyclohydrolase (IMPCH) domain (residues 1-599)
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: 10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase. Bioactivity of the unnatural isomer [6R]-5-formyltetrahydrofolate is in vivo converted to 10-formyl-7,8-dihydrofolate and serves thus as a substrate
Products: -
Products: -
?
additional information
?
-
Q6IN16
Substrates: the enzyme forms a complex with its substrate via the phosphate-binding pocket of the IMP cyclohydrolase (IMPCH) domain (residues 1-599)
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
N10-formyltetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: 10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase
Products: -
Products: -
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: 10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
Substrates: penultimate step of the purine de novo synthesis pathway
Products: -
Products: -
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: precursors for inosinic acid biosynthesis
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: penultimate and final steps in the de novo purine biosynthesis pathway
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: de novo synthesis of purine nucleotides
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: reduced folate cofactor requiring step of de novo purine biosynthesis
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
Substrates: penultimate and final steps in the de novo purine biosynthesis pathway
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: penultimate and final steps in the de novo purine biosynthesis pathway
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: de novo synthesis of purine nucleotides
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: reduced folate cofactor requiring step of de novo purine biosynthesis
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: de novo synthesis of purine nucleotides
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans ATCC 208821
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans CBS 10515
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cryptococcus neoformans FGSC 9487
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Q6IN16
Substrates: -
Products: -
Products: -
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Substrates: -
Products: -
Products: -
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: polymorphisms in 5-aminoimidazole-4-carboxamide ribonucleotide transformylase gene is not associated with recurrent venous thrombosis risk
Products: -
Products: -
?
additional information
?
-
-
Substrates: 10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase. Bioactivity of the unnatural isomer [6R]-5-formyltetrahydrofolate is in vivo converted to 10-formyl-7,8-dihydrofolate and serves thus as a substrate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme forms a complex with its substrate via the phosphate-binding pocket of the IMP cyclohydrolase (IMPCH) domain (residues 1-599)
Products: -
Products: -
?
additional information
?
-
-
Substrates: 10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase. Bioactivity of the unnatural isomer [6R]-5-formyltetrahydrofolate is in vivo converted to 10-formyl-7,8-dihydrofolate and serves thus as a substrate
Products: -
Products: -
?
additional information
?
-
Q6IN16
Substrates: the enzyme forms a complex with its substrate via the phosphate-binding pocket of the IMP cyclohydrolase (IMPCH) domain (residues 1-599)
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N10-formyl-7,8-dihydrofolate
-
kinetically preferred over 10-formyl-5,6,7,8-tetrahydrofolate by AICAR transformylase
N10-formyl-7,8-dihydrofolate
-
kinetically preferred over 10-formyl-5,6,7,8-tetrahydrofolate by AICAR transformylase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
bound in hexacoordinate state to subdomain 3 in each monomer, might a key role in stabilization of the tertiary structure
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2RS)-N-[4-{1-(acetamideoxy)-3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)prop-2-yl}benzoyl]-L-glutamic acid
-
-
(2RS)-N-[4-{1-(acetoxy)-3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)prop-2-yl}benzoyl]-L-glutamic acid
-
-
(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1,1-(dimethoxy)prop-2-yl}benzoyl]-L-glutamic acid
-
-
(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(1,1-bromoacetoxy)prop-2-yl}benzoyl]-L-glutamic acid
-
-
(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(1,1-dimethoxyacetoxy)prop-2-yl}benzoyl]-L-glutamic acid
-
-
(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(ethoxalyoxy) prop-2-yl}benzoyl]-L-glutamic acid
-
-
(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(formyloxy)prop-2-yl}benzoyl]-L-glutamic acid
-
-
(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(hydroxy)prop-2-yl}benzoyl]-L-glutamic acid
-
-
(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(pyruvoyloxy)prop-2-yl}benzoyl]-L-glutamic acid
-
-
(4-(3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)propyl)thiophene-2-carbonyl)-L-glutamic acid
-
(4-(4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl)thiophene-2-carbonyl)-L-glutamic acid
-
(5-(3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)propyl)thiophene-2-carbonyl)-L-glutamic acid
-
(5-(3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)propyl)thiophene-3-carbonyl)-L-glutamic acid
docking and molecular modeling studies of inhibitors N-[4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid, (5-(4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl)thiophene-2-carbonyl)-L-glutamic acid, and (5-(3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)propyl)thiophene-3-carbonyl)-L-glutamic acid with human AICARFTase crystal structure (PDB ID 1P4R)
(5-(4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl)furan-2-carbonyl)-L-glutamic acid
-
(5-(4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl)thiophene-2-carbonyl)-L-glutamic acid
docking and molecular modeling studies of inhibitors N-[4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid, (5-(4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl)thiophene-2-carbonyl)-L-glutamic acid, and (5-(3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)propyl)thiophene-3-carbonyl)-L-glutamic acid with human AICARFTase crystal structure (PDB ID 1P4R)
(5-(4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl)thiophene-3-carbonyl)-L-glutamic acid
-
(S)-2-(4-((2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl)benzamido)pentanedioic acid
-
-
(S)-2-(4-(2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl)benzamido)pentanedioic acid
-
-
(S)-2-(4-(3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)propyl)benzamido)pentanedioic acid
-
-
(S)-2-(4-(4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)butyl)benzamido)pentanedioic acid
-
-
(S)-2-(4-(5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)pentyl)benzamido)pentanedioic acid
-
-
(S)-2-(4-(6-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)hexyl)benzamido)pentanedioic acid
-
-
(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
(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
(S)-2-[2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-acetylamino]-pentanedioic acid
-
-
(S)-2-[2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-acetylamino]-pentanedioic acid
-
-
(S)-2-[3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-propionylamino]-pentanedioic acid
-
-
(S)-2-[3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-propionylamino]-pentanedioic acid
-
-
(S)-2-[4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-benzoylamino]-pentanedioic acid
-
-
(S)-2-[4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-butyrylamino]-pentanedioic acid
-
-
(S)-2-[5-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-pentanoylamino]-pentanedioic acid
-
-
(S)-2-[6-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-hexanoylamino]-pentanedioic acid
-
-
1-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetyl]-piperidine-4-carboxylic acid (pyridin-3-ylmethyl)-amide
-
-
2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-N-[[(pyridin-3-ylmethyl)-carbamoyl]-methyl]-acetamide
-
-
2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-2-ylmethyl-acetamide
-
-
2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-3-ylmethyl-acetamide
-
-
2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-4-ylmethyl-acetamide
-
-
2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
Acid Yellow 54, 326203-A, competitive against 10-formyltetrahydrofolate, IC50: 0.012 mM, inhibitor partially blocks the cofactor binding site
2-[[([4-[2-(2,4-diamino-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]phenyl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
-
weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
2-[[([4-[2-(2,4-diaminopyrido[3,2-d]pyrimidin-6-yl)ethyl]phenyl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
-
weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
2-[[([4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2-fluorophenyl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
-
weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
2-[[([4-[2-(2-amino-4-methylquinazolin-6-yl)ethyl]phenyl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
-
weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
2-[[([5-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2,5-dihydrothiophen-2-yl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
-
weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-propionamide
-
-
3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-2-ylmethyl-propionamide
-
-
3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-3-ylmethyl-propionamide
-
-
3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-4-ylmethyl-propionamide
-
-
4-([2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-methyl)-N-pyridin-3-ylmethyl-benzamide
-
inhibition of thymidylate synthase, as well as glycinamide ribonucleotide formyltransferase and ribonucleotide formyltransferase. Growth inhibition of 4-([2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-methyl)-N-pyridin-3-ylmethyl-benzamide toward KB cells results in cytotoxicity and G1/G2-phase accumulation, and is partially protected by excess thymidine and adenosine, but is completely reversed in the combination of thymidine and adenosine
4-8[2-(2-amino-4-oxo-4,4a,7,7a-tetrahydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)acetamido]methyl]-N-[(pyridin-3-yl)methyl]benzamide
-
-
4-amino-10-methylpteroyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
-
methotrexate polyglutamate, competitive inhibitor
4-amino-4-deoxy-5,8,10-trideazapteroyl-D,L-40-methyleneglutamic acid
-
weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
4-chloro-N-(1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl)benzene-1-sulfonamide
-
4-cyano-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)benzene-1-sulfonamide
-
4-[(2-hydroxy-1-naphthalenyl)azo]benzenesulfonic acid
HNBSA
4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-cyclohexanecarboxylic acid (pyridin-3-ylmethyl)-amide
-
-
4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-benzamide
-
-
4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-butyramide
-
-
5-(5,5-dimethyl-6-oxo-1,4-dihydropyridin-3-yl)-N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)thiophene-2-sulfonamide
-
5-(5-ethyl-5-methyl-6-oxo-1,4-dihydropyridin-3-yl)-N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)thiophene-2-sulfonamide
-
5-[(3R,4S)-3-fluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
-
5-[(3S,4R)-3-fluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
-
5-[(4R)-3,3-difluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
-
5-[(4S)-3,3-difluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
-
5-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-pentanoic acid (pyridin-3-ylmethyl)-amide
-
-
6-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-hexanoic acid (pyridin-3-ylmethyl)-amide
-
-
Cappsin 1
-
non-competitive, inhibition of activity by preventing the formation of dimers
Cappsin 2
-
some derivatives of Cappepsin are also inhibitory, inhibition of activity by preventing the formation of dimers
N-(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)-4-cyanobenzene-1-sulfonamide
-
N-(3-[[2-(2-amino-4-oxo-4,4a,7,7a-tetrahydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]sulfanyl]propanoyl)-L-glutamic acid
-
-
N-(4-[3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-propyl]benzoyl)-L-glutamic acid
-
dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-butyl]benzoyl)-L-glutamic acid
-
dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[5-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-pentyl]benzoyl)-L-glutamic acid
-
dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[6-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-hexyl]benzoyl)-L-glutamic acid
-
dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
-
-
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamylglutamic acid
-
-
N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-(4-hydroxypiperidin-1-yl)thiophene-2-sulfonamide
-
N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide
LSN 3213128, potent and selective inhibitor
N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-(6-oxo-1H-pyridin-3-yl)thiophene-2-sulfonamide
-
N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-[(3R)-3-hydroxy-1-piperidyl]thiophene-2-sulfonamide
-
N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-[(3S)-3-hydroxy-1-piperidyl]thiophene-2-sulfonamide
-
N-([5-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2,3-dihydrothiophen-2-yl]carbonyl)-4-methylideneglutamic acid
-
-
N-([[2-(2-amino-4-oxo-4,4a,7,7a-tetrahydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]sulfanyl]acetyl)-L-glutamic acid
-
-
N-[(4-[[(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)amino]sulfonyl]-phenyl)carbonyl]-L-glutamic acid
-
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
N-[4-[2-(2,4-diamino-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminopyrido[3,2-d]pyrimidin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2-fluorobenzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2-amino-4-methylquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[3-(2-amino-4-oxo-3,4-dihydrothieno[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
inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
N-[4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
docking and molecular modeling studies of inhibitors N-[4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid, (5-(4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl)thiophene-2-carbonyl)-L-glutamic acid, and (5-(3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)propyl)thiophene-3-carbonyl)-L-glutamic acid with human AICARFTase crystal structure (PDB ID 1P4R)
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)butyl]benzoyl]glutamic acid
AGF23
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
permetrexate
PMX, an iconic C1 inhibitor, is a 5-substituted pyrrolo[2,3-d]pyrimidine with a 2-carbon bridge which is linked to a p-aminobenzoyl-L-glutamate
-
4-amino-10-methylpteroylglutamic acid
-
methotrexate, non-competitive inhibitor
4-amino-10-methylpteroylglutamic acid
methotrexate, non-competitive inhibitor
4-amino-10-methylpteroylglutamic acid
-
methotrexate, non-competitive inhibitor
methotrexate
enzyme phosphorylation dampens the methotrexate-mediated transformylase activity inhibition
pemetrexed
the enzyme is a pharmacologically important target of anticancer drug pemetrexed, an antifolate inhibitor
additional information
dissociation constants of the enzyme inhibitors, molecular docking study, and molecular dynamics simulation analysis, overview. The inhibitors exhibit hydrophobic interactions along with hydrogen bonding
-
additional information
-
specific antifolate reagents and nonfolate inhibitors are analogues of cofactor N10-formyltetrahydrofolate and can completely inhibit AICAR Tfase activity
-
additional information
-
methotrexate, MTX, cannot directly inhibit AICAR transformylase, but blocks the AICAR transformylase process in patients with rheumatoid arthritis
-
additional information
-
synthesis and antitumor activity of a series of 6-substituted pyrrolo[2,3-d]pyrimidines as potential nonclassical antifolates targeting both thymidylate and purine nucleotide biosynthesis, docking study and molecular modeling using the enzyme's crystal structure in complex with compound BW2315, PDB ID 1PL0. Growth inhibition of human cancer cells by the inhibitors, IC50 values, overview
-
additional information
-
synthesis of 5-substituted pyrrolo[2,3-d]pyrimidine antifolate inhibitors that acts as a dual inhibitor of GARFTase, EC 2.1.2.2, and AICARFTase principal mechanism of action, overview. 8, with a 4-carbon bridge, is the most active analog and potently inhibits proliferation of folate receptor alpha-expressing Chinese hamster ovary and KB human tumor cells. Molecular modeling and docking studies, overview
-
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
-
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
-
additional information
6-substituted thieno[2,3-d]pyrimidine analogues as dual inhibitors of 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthesis in folate receptor expressing human tumors, synthesis and structure-activity studies, molecular docking and modeling, overview; growth inhibition study of CHO cells expressing the human enzyme as well as the folate receptor
-
additional information
-
an adventitiously active site-bound nucleotide, found in the crystal structures, is identified by NMR and mass spectral analysis as a novel 5-formyl derivative of an earlier intermediate in the biosynthetic pathway 4-carboxy-5-aminoimidazole ribonucleotide. The nucleotide is a cyclohydrolase inhibitor. Binding structure analysis, structure modeling, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzyme phosphorylation by anaplastic lymphoma kinase enhances enzymatic activity and dampens the methotrexate-mediated transformylase activity inhibition
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Cellular Pharmacodynamics of a Novel Pyrrolo[3,2-d]pyrimidine Inhibitor Targeting Mitochondrial and Cytosolic One-Carbon Metabolism.
Arthritis
5-Aminoimidazole-4-carboxamide ribonucleotide-transformylase and inosine-triphosphate-pyrophosphatase genes variants predict remission rate during methotrexate therapy in patients with juvenile idiopathic arthritis.
Arthritis
Association of the 5-aminoimidazole-4-carboxamide ribonucleotide transformylase gene with response to methotrexate in juvenile idiopathic arthritis.
Arthritis, Juvenile
5-Aminoimidazole-4-carboxamide ribonucleotide-transformylase and inosine-triphosphate-pyrophosphatase genes variants predict remission rate during methotrexate therapy in patients with juvenile idiopathic arthritis.
Arthritis, Juvenile
Association of the 5-aminoimidazole-4-carboxamide ribonucleotide transformylase gene with response to methotrexate in juvenile idiopathic arthritis.
Arthritis, Rheumatoid
Association of the ATIC 347 C/G polymorphism with responsiveness to and toxicity of methotrexate in rheumatoid arthritis: a meta-analysis.
Arthritis, Rheumatoid
Effects of methotrexate on nucleotide pools in normal human T cells and the CEM T cell line.
Arthritis, Rheumatoid
Evidence for the hypothesis that 10-formyldihydrofolate is the in vivo substrate for aminoimidazolecarboxamide ribotide transformylase.
Arthritis, Rheumatoid
Metabolism-blocked antifolates as potential anti-rheumatoid arthritis agents: 4-amino-4-deoxy-5,8,10-trideazapteroyl-d,l-4'-methyleneglutamic acid (CH-1504) and its analogs.
Ataxia Telangiectasia
DNA-dependent protein kinase regulates lysosomal AMP-dependent protein kinase activation and autophagy.
Breast Neoplasms
Proteomic analysis of human macrophages exposed to hypochlorite-oxidized low-density lipoprotein.
Breast Neoplasms
Targeting tumour proliferation with a small-molecule inhibitor of AICAR transformylase homodimerization.
Carcinogenesis
The Adenosine Monophosphate (AMP) Analog, 5-Aminoimidazole-4-Carboxamide Ribonucleotide (AICAR) Inhibits Hepatosteatosis and Liver Tumorigenesis in a High-Fat Diet Murine Model Treated with Diethylnitrosamine (DEN).
Carcinoma
Identification of a Small Molecule Inhibitor of RAD52 by Structure-Based Selection.
Carcinoma, Hepatocellular
The Adenosine Monophosphate (AMP) Analog, 5-Aminoimidazole-4-Carboxamide Ribonucleotide (AICAR) Inhibits Hepatosteatosis and Liver Tumorigenesis in a High-Fat Diet Murine Model Treated with Diethylnitrosamine (DEN).
Diabetes, Gestational
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Fetal Growth Retardation
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Graft vs Host Disease
Cyclosporine and methotrexate-related pharmacogenomic predictors of acute graft-versus-host disease.
Huntington Disease
AMPK activation protects from neuronal dysfunction and vulnerability across nematode, cellular and mouse models of Huntington's disease.
Huntington Disease
AMPK-dependent phosphorylation is required for transcriptional activation of TFEB and TFE3.
Infections
The Mesorhizobium loti purB gene is involved in infection thread formation and nodule development in Lotus japonicus.
Insulin Resistance
Serum Is Not Necessary for Prior Pharmacological Activation of AMPK to Increase Insulin Sensitivity of Mouse Skeletal Muscle.
Kidney Failure, Chronic
Podocytes maintain high basal levels of autophagy independent of mtor signaling.
Leukemia
5-Aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase from human CCRF-CEM leukemia cells: purification, pH dependence, and inhibitors.
Leukemia
Dual effects of pyrazofurin and 3-deazauridine upon pyrimidine and purine biosynthesis in mouse L1210 leukemia.
Lung Injury
AICAR decreases acute lung injury by phosphorylating AMPK and upregulating heme oxygenase-1.
Neoplasms
AMPK-dependent phosphorylation is required for transcriptional activation of TFEB and TFE3.
Neoplasms
Characterization of a novel AICARFT inhibitor which potently elevates ZMP and has anti-tumor activity in murine models.
Neoplasms
Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide transformylase in complex with a novel non-folate inhibitor identified by virtual ligand screening.
Neoplasms
Discovery of 6-substituted thieno[2,3-d]pyrimidine analogs as dual inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthesis in folate receptor expressing human tumors.
Neoplasms
Discovery of N-(6-Fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), a Potent and Selective Nonclassical Antifolate Aminoimidazole-4-carboxamide Ribonucleotide Formyltransferase (AICARFT) Inhibitor Effective at Tumor Suppression in a Cancer Xenograft Model.
Neoplasms
DNA-dependent protein kinase regulates lysosomal AMP-dependent protein kinase activation and autophagy.
Neoplasms
Peptide YY (PYY) Is Expressed in Human Skeletal Muscle Tissue and Expanding Human Muscle Progenitor Cells.
Neoplasms
STYK1 promotes autophagy through enhancing the assembly of autophagy-specific class III phosphatidylinositol 3-kinase complex I.
Neoplasms
Targeting tumour proliferation with a small-molecule inhibitor of AICAR transformylase homodimerization.
Ovarian Neoplasms
Activation of AMP-activated Protein Kinase by Metformin Induces Protein Acetylation in Prostate and Ovarian Cancer Cells.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Novel pyrrolo[2,3-d]pyrimidine antifolate TNP-351: cytotoxic effect on methotrexate-resistant CCRF-CEM cells and inhibition of transformylases of de novo purine biosynthesis.
Pregnancy Complications
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Premature Birth
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Psoriasis
Outcomes of methotrexate therapy for psoriasis and relationship to genetic polymorphisms.
Sepsis
Activation of AMP-activated protein kinase during sepsis/inflammation improves survival by preserving cellular metabolic fitness.
Starvation
Metabolomics profiling of metformin-mediated metabolic reprogramming bypassing AMPK?.
Tuberculosis
Structural analyses of a purine biosynthetic enzyme from Mycobacterium tuberculosis reveal a novel bound nucleotide.
Tuberous Sclerosis
Podocytes maintain high basal levels of autophagy independent of mtor signaling.
Venous Thrombosis
Associations of common polymorphisms in the thymidylate synthase, reduced folate carrier and 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase genes with folate and homocysteine levels and venous thrombosis risk.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.245
10-formyldihydrofolate
pH 7.5, temperature not specified in the publication
0.0009
5-amino-imidazole-4-thiocarboxamide ribonucleotide
-
10-formyldihydrofolate as cofactor
0.111
10-formyltetrahydrofolate
pH 7.5, temperature not specified in the publication
0.13437
10-formyltetrahydrofolate
AICAR transformylase activity of domain truncation mutant pET-28c-AICARTF1, pH 7.4, temperature not specified in the publication
0.138
10-formyltetrahydrofolate
full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication
0.13824
10-formyltetrahydrofolate
at pH 7.4, temperature not specified in the publication
0.1466
10-formyltetrahydrofolate
pH 8.2, 37°C, AICAR TFase activity of CLasATIC
0.01
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
66 mM Tris, pH 7.4, 50 mM KCl, temperature not specified in the publication
0.016
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
dextran-rich phase, at pH 7.4, temperature not specified in the publication
0.0168
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
33 mM Tris, pH 7.4, 25 mM KCl, temperature not specified in the publication
0.019
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
PEG-rich phase, at pH 7.4, temperature not specified in the publication
0.03243
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
at pH 7.4, temperature not specified in the publication
0.034
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 8.2, 37°C, AICAR TFase activity of CLasATIC
0.0346
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
at pH 7.5 and 25°C
0.03468
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
AICAR transformylase activity of domain truncation mutant pET-28c-AICARTF1, pH 7.4, temperature not specified in the publication
0.13
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, 37°C, AICAR TFase
0.3243
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication
0.0015
5-aminoimidazole-4-carboxamide ribonucleotide
-
10-formyldihydrofolate as cofactor
0.0019
5-aminoimidazole-4-carboxamide ribonucleotide
-
10-formyltetrahydrofolate as cofactor
0.0021
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
at pH 7.4, temperature not specified in the publication
0.03
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, 37°C, AICAR TFase
additional information
additional information
-
10-formyl-7,8-dihydrofolate has an about 5fold kinetic advantage, Vm/Km, over 10-formyl-5,6,7,8-tetrahydrofolate for AICAR transformylases in human leukemia cells and for human recombinant AICAR transformylase
-
additional information
additional information
-
10-formyl-7,8-dihydrofolate has an about 5fold kinetic advantage, Vm/Km, over 10-formyl-5,6,7,8-tetrahydrofolate for AICAR transformylases in rat bone marrow cells
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.18
10-formyldihydrofolate
pH 7.5, temperature not specified in the publication
7.7
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, 37°C, AICAR TFase
0.311
10-formyltetrahydrofolate
pH 8.2, 37°C, AICAR TFase activity of CLasATIC
4.97
10-formyltetrahydrofolate
pH 7.5, temperature not specified in the publication
0.311
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 8.2, 37°C, AICAR TFase activity of CLasATIC
2.9
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
66 mM Tris, pH 7.4, 50 mM KCl, temperature not specified in the publication
3.63
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
at pH 7.5 and 25°C
6.5
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
PEG-rich phase, at pH 7.4, temperature not specified in the publication
7
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
dextran-rich phase, at pH 7.4, temperature not specified in the publication
7.5
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, 37°C, AICAR TFase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.3
10-formyldihydrofolate
pH 7.5, temperature not specified in the publication
256.7
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, 37°C, AICAR TFase
2.12
10-formyltetrahydrofolate
pH 8.2, 37°C, AICAR TFase activity of CLasATIC
44.77
10-formyltetrahydrofolate
pH 7.5, temperature not specified in the publication
9.15
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 8.2, 37°C, AICAR TFase activity of CLasATIC
57.7
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, 37°C, AICAR TFase
4150
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
at pH 7.5 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
pH 7.5
0.00088
permetrexate
pH and temperature not specified in the publication
-
additional information
additional information
inhibition kinetics
-
0.2
methotrexate
above, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
Gallus gallus
Acid Yellow 54, 326203-A, competitive against 10-formyltetrahydrofolate, IC50: 0.012 mM, inhibitor partially blocks the cofactor binding site
0.0348
4-chloro-N-(1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl)benzene-1-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.000608
4-cyano-N-(1-oxo-1,2-dihydroisoquinolin-7-yl)benzene-1-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.000723
4-cyano-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)benzene-1-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.1
4-cyano-N-phenylbenzene-1-sulfonamide
Homo sapiens
IC50 above 0.1 mM, at pH 7.5 and 25°C
0.000005
5-(5,5-dimethyl-6-oxo-1,4-dihydropyridin-3-yl)-N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)thiophene-2-sulfonamide
Homo sapiens
IC50 below 0.000005 mM, at pH 7.5 and 25°C
0.000005
5-(5-ethyl-5-methyl-6-oxo-1,4-dihydropyridin-3-yl)-N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)thiophene-2-sulfonamide
Homo sapiens
IC50 below 0.000005 mM, at pH 7.5 and 25°C
0.00002
5-[(3R,4S)-3-fluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.0000078
5-[(3S,4R)-3-fluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.000012
5-[(4R)-3,3-difluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.000013
5-[(4S)-3,3-difluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.0181
N-(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)-4-cyanobenzene-1-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.000013
N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-(4-hydroxypiperidin-1-yl)thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.000014 - 0.000016
N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide
0.000005
N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-(6-oxo-1H-pyridin-3-yl)thiophene-2-sulfonamide
Homo sapiens
IC50 below 0.000005 mM, at pH 7.5 and 25°C
0.000026
N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-[(3R)-3-hydroxy-1-piperidyl]thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.000018
N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-[(3S)-3-hydroxy-1-piperidyl]thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
additional information
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)glutamic acid
0.000014
N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.000016
N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide
Homo sapiens
at pH 7.5 and 25°C
additional information
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)glutamic acid
Homo sapiens
-
value above 0.05
additional information
N-([5-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2,3-dihydrothiophen-2-yl]carbonyl)-4-methylideneglutamic acid
Homo sapiens
-
value above 0.05
additional information
N-[4-[2-(2,4-diamino-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]benzoyl]-4-methylideneglutamic acid
Homo sapiens
-
value above 0.05
additional information
N-[4-[2-(2,4-diaminopyrido[3,2-d]pyrimidin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
Homo sapiens
-
value above 0.05
additional information
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2-fluorobenzoyl]-4-methylideneglutamic acid
Homo sapiens
-
value above 0.05
additional information
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
Homo sapiens
-
value above 0.05
additional information
N-[4-[2-(2-amino-4-methylquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
Homo sapiens
-
value above 0.05
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0496
crude enzyme, at pH 7.4, temperature not specified in the publication
0.973
after 19.62fold purification, at pH 7.4, temperature not specified in the publication
additional information
-
1 unit = removal of 0.0001 mM of AICA-ribotide/0.5 ml/20 min at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
7.8
AICAR transformylase activity of the bifunctional enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
pH 6.5: about 50% of maximal activity, pH 9.5: about 50% of maximal activity, AICAR transformylase activity of the bifunctional enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
37
35
AICAR transformylase activity of the bifunctional enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
20°C: about 40% of maximal activity, 50°C: about 40% of maximal activity, AICAR transformylase activity of the bifunctional enzyme
25 - 45
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Filobasidiella neoformans var. grubii, serotype A
SwissProt
brenda
Cryptococcus neoformans ATCC 208821
Filobasidiella neoformans var. grubii, serotype A
SwissProt
brenda
Cryptococcus neoformans CBS 10515
Filobasidiella neoformans var. grubii, serotype A
SwissProt
brenda
Cryptococcus neoformans FGSC 9487
Filobasidiella neoformans var. grubii, serotype A
SwissProt
brenda
Filobasidiella neoformans var. grubii, serotype A
SwissProt
brenda
bifunctional 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme later accumulates in the Golgi/endosome network
brenda
Q6IN16
the enzyme later accumulates in the Golgi/endosome network
brenda
the enzyme later accumulates in the Golgi/endosome network
brenda
Q6IN16
the enzyme later accumulates in the Golgi/endosome network
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the ATIC enzyme from the plant pathogen Candidatus Liberibacter asiaticus belongs to the AICAR transformylase/IMP cyclohydrolase purH superfamily
evolution
-
the ATIC enzyme from the plant pathogen Candidatus Liberibacter asiaticus belongs to the AICAR transformylase/IMP cyclohydrolase purH superfamily
-
malfunction
inhibition of the enzyme results in depletion of purine nucleotides
malfunction
insulin stimulation and enzyme ATIC knockdown readily increase the level of AMP-activated protein kinase-Thr172 phosphorylation in insulin receptor complexes. Enzyme ATIC, protein-tyrosine phosphatase-like A domain-containing protein 1, and AMP-activated protein kinase knockdown affects insulin receptor internalization in HEK-293 cells
malfunction
Q6IN16
insulin stimulation and enzyme ATIC knockdown readily increase the level of AMPK-Thr172 phosphorylation in insulin receptor complexes
malfunction
the ATIC rs2372536 GG enzyme genotype is associated with improved clinical remission in juvenile idiopathic arthritis during methotrexate therapy, only one of the ATIC single nucleotide polymorphisms show any trend toward methotrexate response in an independent cohort of North American juvenile idiopathic arthritis children
malfunction
growth deficiency phenotypes (in un-supplemented M9 minimal medium containing thymidine) are direct consequences of the gene deletions
malfunction
mutants lacking the ATIC-encoding ADE16 gene are adenine and histidine auxotrophs that are unable to establish an infection in a murine model of virulence. Loss of ATIC results in an accumulation of AICAR and a negative feedback loop that inhibits ATP phosphoribosyltransferase, the first enzyme of histidine biosynthesis, resulting in histidine auxotrophy
malfunction
ATIC is a bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Upper tract urothelial carcinoma (UTUC), including renal, pelvic, and ureteral carcinoma, has a high incidence rate in Taiwan. High ATIC expression is associated with tumor stage, metastasis, recurrence, and a poor prognosis in patients with UTUC. ATIC knockdown inhibits the proliferation, migration, and invasive abilities of UTUC cells, e.g. BFTC909, UM-UC-14, and KMPC3 cells. In contrast, miR-145-5p affects the proliferation, migration, and invasive abilities of UTUC cells by directly targeting the 3'-untranslated regions of ATIC. ATIC is overexpressed in hepatocellular carcinoma, myeloma, and lung adenocarcinoma tissues and is correlated with a poor prognosis
malfunction
-
growth deficiency phenotypes (in un-supplemented M9 minimal medium containing thymidine) are direct consequences of the gene deletions
-
malfunction
Cryptococcus neoformans ATCC 208821
-
mutants lacking the ATIC-encoding ADE16 gene are adenine and histidine auxotrophs that are unable to establish an infection in a murine model of virulence. Loss of ATIC results in an accumulation of AICAR and a negative feedback loop that inhibits ATP phosphoribosyltransferase, the first enzyme of histidine biosynthesis, resulting in histidine auxotrophy
-
malfunction
Cryptococcus neoformans CBS 10515
-
mutants lacking the ATIC-encoding ADE16 gene are adenine and histidine auxotrophs that are unable to establish an infection in a murine model of virulence. Loss of ATIC results in an accumulation of AICAR and a negative feedback loop that inhibits ATP phosphoribosyltransferase, the first enzyme of histidine biosynthesis, resulting in histidine auxotrophy
-
malfunction
Cryptococcus neoformans FGSC 9487
-
mutants lacking the ATIC-encoding ADE16 gene are adenine and histidine auxotrophs that are unable to establish an infection in a murine model of virulence. Loss of ATIC results in an accumulation of AICAR and a negative feedback loop that inhibits ATP phosphoribosyltransferase, the first enzyme of histidine biosynthesis, resulting in histidine auxotrophy
-
malfunction
-
mutants lacking the ATIC-encoding ADE16 gene are adenine and histidine auxotrophs that are unable to establish an infection in a murine model of virulence. Loss of ATIC results in an accumulation of AICAR and a negative feedback loop that inhibits ATP phosphoribosyltransferase, the first enzyme of histidine biosynthesis, resulting in histidine auxotrophy
-
metabolism
-
aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis. No enzyme complex that generates 10-formyl-5,6,7,8-tetrahydrofolate and immediately channels or furnishes it to AICAR transformylase is needed because the first oxidation product of 10-formyl-5,6,7,8-tetrahydrofolate is 10-formyl-7,8-dihydrofolate that is utilized by this transformylase
metabolism
-
aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis
metabolism
last and rate-limiting enzyme of the de novo purine synthesis pathway
metabolism
Q6IN16
last and rate-limiting enzyme of the de novo purine synthesis pathway
metabolism
the enzyme AICAR-transformylase/IMP cyclohydrolase (ATIC) catalyzes the last two steps of purine de novo synthesis. High glucose up-regulates the expression and activity of the enzyme and increases the levels of reactive oxygen species and methylglyoxal-derived advanced glycation end products. Overexpression of the enzyme (atic-1) decreases the lifespan and head motility and increases neuronal damage under both standard and high glucose conditions. Inhibition of atic-1 expression, by RNAi, under high glucose is associated with increased lifespan and head motility and reduced neuronal damage, reactive oxygen species, and methylglyoxal-derived advanced glycation end product accumulation. The enzyme (atic-1) is involved in glucotoxic effects under high glucose conditions, either by blocked atic-1 expression or via induction of 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) and AMP-activated kinase (AMPK) induction
metabolism
the 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase/inosine monophosphate (IMP) cyclohydrolase (ATIC) catalyzes final two steps of purine nucleotide de novo biosynthetic pathway. The cell proliferation activity of the enzyme is observed where it promotes proliferation and viability of NIH 3T3 and RIN-5F cells, exhibits in vitro wound healing in NIH 3T3 fibroblast cells, and rescues RIN-5F cells from the cytotoxic effects of palmitic acid and high glucose
metabolism
the bifunctional enzyme is involved in catalyzing penultimate and final steps of purine de novo biosynthetic pathway crucial for the survival of organisms. De novo synthesis is the main pathway required for the formation of inosine monophosphate (IMP) from simple molecule precursors and comprises ten steps in higher organisms. The final two steps are catalyzed by a single polypeptide bifunctional enzyme, 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase (ATIC), also known as purHJ. The penultimate step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase (AICAR TFase) which transfers the formyl group from the cofactor, (6R) N10-formyl-tetrahydrofolate (10-f-THF), to the exocyclic 5-amino group of AICAR to form 5-formyl-AICAR (FAICAR)
metabolism
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans
metabolism
miR-145-5p regulates the protein levels of fibronectin 1, Slug, cyclin A2, cyclin B1, P57, and interferon-induced transmembrane 1 via ATIC
metabolism
Cryptococcus neoformans ATCC 208821
-
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans
-
metabolism
-
the bifunctional enzyme is involved in catalyzing penultimate and final steps of purine de novo biosynthetic pathway crucial for the survival of organisms. De novo synthesis is the main pathway required for the formation of inosine monophosphate (IMP) from simple molecule precursors and comprises ten steps in higher organisms. The final two steps are catalyzed by a single polypeptide bifunctional enzyme, 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase (ATIC), also known as purHJ. The penultimate step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase (AICAR TFase) which transfers the formyl group from the cofactor, (6R) N10-formyl-tetrahydrofolate (10-f-THF), to the exocyclic 5-amino group of AICAR to form 5-formyl-AICAR (FAICAR)
-
metabolism
Cryptococcus neoformans CBS 10515
-
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans
-
metabolism
Cryptococcus neoformans FGSC 9487
-
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans
-
metabolism
-
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans
-
physiological function
-
10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase, an enzyme in purine nucleotide biosynthesis de novo, which introduces C2 into the purine ring
physiological function
-
10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase, an enzyme in purine nucleotide biosynthesis de novo, which introduces C2 into the purine ring
physiological function
the enzyme is involved in purine nucleotide biosynthesis
physiological function
the enzyme 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase plays a central role in insulin signaling and the Golgi/endosomes protein network, compartmentalization in vivo of involved enzymes in response to insulin, kinetics of the localization, overview
physiological function
Q6IN16
the enzyme 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase plays a central role in insulin signaling and the Golgi/endosomes protein network, compartmentalization in vivo of involved enzymes in response to insulin, kinetics of the localization, overview
physiological function
the bicuntional enzyme ATIC accelerates wound healing of NIH-3T3 fibroblasts by inducing proliferation and migration
physiological function
enzyme overexpression decreases the median lifespan from 23.6 to 20.6 days compared with control nematodes under standard conditions
physiological function
the bifunctional enzyme from Liberibacter asiaticus CLasATIC or 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase/inosine monophosphate (IMP) cyclohydrolase (ATIC) is involved in catalyzing penultimate and final steps of purine de novo biosynthetic pathway crucial for the survival of organisms. The bifunctional enzyme catalyzes both the AICAR TFase and IMPCHase activities, respectively
physiological function
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans, it catalyzes the final two enzymatic steps in the formation of the first purine base inosine monophosphate. ADE16 is essential for adenine and histidine prototrophy in Cryptococcus neoformans
physiological function
ATIC is a bifunctional enzyme that catalyzes the last two steps of purine biosynthesis
physiological function
Cryptococcus neoformans ATCC 208821
-
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans, it catalyzes the final two enzymatic steps in the formation of the first purine base inosine monophosphate. ADE16 is essential for adenine and histidine prototrophy in Cryptococcus neoformans
-
physiological function
-
the bifunctional enzyme from Liberibacter asiaticus CLasATIC or 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase/inosine monophosphate (IMP) cyclohydrolase (ATIC) is involved in catalyzing penultimate and final steps of purine de novo biosynthetic pathway crucial for the survival of organisms. The bifunctional enzyme catalyzes both the AICAR TFase and IMPCHase activities, respectively
-
physiological function
Cryptococcus neoformans CBS 10515
-
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans, it catalyzes the final two enzymatic steps in the formation of the first purine base inosine monophosphate. ADE16 is essential for adenine and histidine prototrophy in Cryptococcus neoformans
-
physiological function
Cryptococcus neoformans FGSC 9487
-
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans, it catalyzes the final two enzymatic steps in the formation of the first purine base inosine monophosphate. ADE16 is essential for adenine and histidine prototrophy in Cryptococcus neoformans
-
physiological function
-
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans, it catalyzes the final two enzymatic steps in the formation of the first purine base inosine monophosphate. ADE16 is essential for adenine and histidine prototrophy in Cryptococcus neoformans
-
additional information
-
the enzyme is located at the C-terminus of the bifunctional purine-biosynthesis protein, PurH, whose N-terminus possesses IMP cyclohydrolase activity. Coupling of the two domains is essential for the catalytic process, as the AICAR Tfase reaction favours the reverse direction by itself and the irreversible cyclization of 5-formyl-aminoimidazole-4-carboxamide ribonucleotide to IMP drives formyl transfer in the forward direction
additional information
-
structure and active site of AICAR transformylase are not consistent with other enzymes that utilize 10-formyl-5,6,7,8-tetrahydrofolate. Methotrexate blockage of the AICAR transformylase process in patients with rheumatoid arthritis suggests that dihydrofolate reductase is involved and is consistent with dihydrofolate and 10-formyl-7,8-dihydrofolate being the product and substrate for AICAR transformylase
additional information
-
structure and active site of AICAR transformylase are not consistent with other enzymes that utilize 10-formyl-5,6,7,8-tetrahydrofolate. Methotrexate blockage of the AICAR transformylase process in patients with rheumatoid arthritis suggests that dihydrofolate reductase is involved and is consistent with dihydrofolate and 10-formyl-7,8-dihydrofolate being the product and substrate for AICAR transformylase
additional information
-
the enzyme is part of the the bifunctional enzyme 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase, ATIC, or PurH
additional information
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide is a is a potent allosteric AMPK activator
additional information
Q6IN16
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide is a is a potent allosteric AMPK activator. Insulin receptor autophosphorylation in isolated endosomes incubated in the presence of purified enzyme ATIC
additional information
residues are Arg226, Tyr227, Glu342, Ser430, Asn431, Ser450, Phe484, Asp490, and Ser509 are involved in AICAR transformylase activity. The two conserved key catalytic residues Lys288 and His289 are essential for AICAR TFase activity, whereby His289 is supposed to act as a catalytic base to deprotonate the AICAR along with the nucleophilic attack on 10-f-THF, while Lys288 helps in the stabilization of the oxyanion transition state and subsequent shuttling of protons to THF as seen in avian ATIC crystal structure
additional information
enzyme structure homology modeling with bound ligands, overview
additional information
active site structure, Cryptococcus neoformans ATIC crystal structure analysis (PDB ID 7MGQ), overview
additional information
-
the enzyme is part of the the bifunctional enzyme 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase, ATIC, or PurH
-
additional information
Cryptococcus neoformans ATCC 208821
-
active site structure, Cryptococcus neoformans ATIC crystal structure analysis (PDB ID 7MGQ), overview
-
additional information
-
residues are Arg226, Tyr227, Glu342, Ser430, Asn431, Ser450, Phe484, Asp490, and Ser509 are involved in AICAR transformylase activity. The two conserved key catalytic residues Lys288 and His289 are essential for AICAR TFase activity, whereby His289 is supposed to act as a catalytic base to deprotonate the AICAR along with the nucleophilic attack on 10-f-THF, while Lys288 helps in the stabilization of the oxyanion transition state and subsequent shuttling of protons to THF as seen in avian ATIC crystal structure
-
additional information
Cryptococcus neoformans CBS 10515
-
active site structure, Cryptococcus neoformans ATIC crystal structure analysis (PDB ID 7MGQ), overview
-
additional information
Cryptococcus neoformans FGSC 9487
-
active site structure, Cryptococcus neoformans ATIC crystal structure analysis (PDB ID 7MGQ), overview
-
additional information
-
active site structure, Cryptococcus neoformans ATIC crystal structure analysis (PDB ID 7MGQ), overview
-
Show AA Sequence and Transmembrane Helices (19054 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
dimer
2 * 61000, recombinant His-tagged enzyme, SDS-PAGE
dimer
-
2 * 61000, recombinant His-tagged enzyme, SDS-PAGE
-
dimer
crystal structure analysis, monomer contains two functionally independent domains transformylase and cyclohydrolase activities
dimer
-
monomer-dimer equilibrium in solution, dimeric form is required for transformylase activity
dimer
crystal structure analysis, monomer contains two functionally independent domains transformylase and cyclohydrolase activities
dimer
2 * 54000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking studies, the purified recombinant enzyme and its truncated domains exist mainly in dimeric form
homodimer
each enzyme monomer has an N-terminal IMP cyclohydrolase domain (residues 1-197) and a C-terminal AICAR transformylase domain (212-605), and the active sites of each are inferred based on sequence alignments and comparison with the ligand-bound structure of the avian and human ATIC enzymes. A 15-residue loop is connecting the IMP cyclohydrolase and AICAR transformylase domains. This loop is located away from the AICAR transformylase and IMP cyclohydrolase active sites and is unlikely to play a role in catalysis but may contribute to the stability of the enzyme dimer and may be targeted with compounds that can selectively bind in ATIC and inhibit the function of the enzyme
homodimer
Cryptococcus neoformans ATCC 208821
-
each enzyme monomer has an N-terminal IMP cyclohydrolase domain (residues 1-197) and a C-terminal AICAR transformylase domain (212-605), and the active sites of each are inferred based on sequence alignments and comparison with the ligand-bound structure of the avian and human ATIC enzymes. A 15-residue loop is connecting the IMP cyclohydrolase and AICAR transformylase domains. This loop is located away from the AICAR transformylase and IMP cyclohydrolase active sites and is unlikely to play a role in catalysis but may contribute to the stability of the enzyme dimer and may be targeted with compounds that can selectively bind in ATIC and inhibit the function of the enzyme
-
homodimer
Cryptococcus neoformans CBS 10515
-
each enzyme monomer has an N-terminal IMP cyclohydrolase domain (residues 1-197) and a C-terminal AICAR transformylase domain (212-605), and the active sites of each are inferred based on sequence alignments and comparison with the ligand-bound structure of the avian and human ATIC enzymes. A 15-residue loop is connecting the IMP cyclohydrolase and AICAR transformylase domains. This loop is located away from the AICAR transformylase and IMP cyclohydrolase active sites and is unlikely to play a role in catalysis but may contribute to the stability of the enzyme dimer and may be targeted with compounds that can selectively bind in ATIC and inhibit the function of the enzyme
-
homodimer
Cryptococcus neoformans FGSC 9487
-
each enzyme monomer has an N-terminal IMP cyclohydrolase domain (residues 1-197) and a C-terminal AICAR transformylase domain (212-605), and the active sites of each are inferred based on sequence alignments and comparison with the ligand-bound structure of the avian and human ATIC enzymes. A 15-residue loop is connecting the IMP cyclohydrolase and AICAR transformylase domains. This loop is located away from the AICAR transformylase and IMP cyclohydrolase active sites and is unlikely to play a role in catalysis but may contribute to the stability of the enzyme dimer and may be targeted with compounds that can selectively bind in ATIC and inhibit the function of the enzyme
-
homodimer
-
each enzyme monomer has an N-terminal IMP cyclohydrolase domain (residues 1-197) and a C-terminal AICAR transformylase domain (212-605), and the active sites of each are inferred based on sequence alignments and comparison with the ligand-bound structure of the avian and human ATIC enzymes. A 15-residue loop is connecting the IMP cyclohydrolase and AICAR transformylase domains. This loop is located away from the AICAR transformylase and IMP cyclohydrolase active sites and is unlikely to play a role in catalysis but may contribute to the stability of the enzyme dimer and may be targeted with compounds that can selectively bind in ATIC and inhibit the function of the enzyme
-
additional information
enzyme CLasATIC is an alpha/beta protein with 37% alpha-helix and 23% beta-sheets, structure comparisons, overview. The AICAR transformylase (AICAR TFase) activity is present in C-terminal domain, while the inosine monophosphate cyclohyrdolase (IMPCHase) activity of the bifunctional enzyme resides in the N-terminal domain
additional information
-
enzyme CLasATIC is an alpha/beta protein with 37% alpha-helix and 23% beta-sheets, structure comparisons, overview. The AICAR transformylase (AICAR TFase) activity is present in C-terminal domain, while the inosine monophosphate cyclohyrdolase (IMPCHase) activity of the bifunctional enzyme resides in the N-terminal domain
-
additional information
-
PurH is composed of two domains linked by a flexible region. The N-terminal domain possesses IMPCH activity and the C-terminal domain possesses AICAR Tfase activity
additional information
-
the protein is folded into two domains, the N-terminal domain, residues 1-212, containing the cyclohydrolase active site and the C-terminal domain, residues 222-523, containing the formyltransferase active site, structure modeling, overview
additional information
-
the protein is folded into two domains, the N-terminal domain, residues 1-212, containing the cyclohydrolase active site and the C-terminal domain, residues 222-523, containing the formyltransferase active site, structure modeling, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
bifunctional 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase associates with nucleoplasmin-anaplastic lymphoma kinase, and its phosphorylation requires anaplastic lymphoma kinase activity. Phosphorylation enhances enzymatic activity and dampens the methotrexate-mediated transformylase activity inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, by hanging drop vapor diffusion, mixing of 12 g/ml protein in 10 mM HEPES, pH 7.5, 150 mM NaCl, and 1 mM DTT, with reservoir solution containing 0.2 M MgCl2, 20% w/v PEG 6000, and 0.2 M Tris base, pH 8.0, 20°C, X-ray diffraction structure determination and analysis at 2.67 A resolution, molecular replacement using the human ATIC structure (PDB ID 1PKX) as search model
purified recombinant His6-tagged PurH, without methylation of the 28 lysine residues, sitting drop vapour diffusion method, mixing of 0.001 ml of 56 mg/ml protein in 0.8 M sodium/potassium hydrogen phosphate, pH 7.5, with 0.001 ml of reservoir solution containing 0.1 M sodium acetate, pH 5.0, 1 M ammonium sulfate, 1 week to 1 month, X-ray diffraction structure determination and analysis at 3.05 A resolution
-
crystallized in complex with its inhibitor 2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
recombinant His-tag fusion protein crystallized by sitting drop vapor diffusion method in complex with its inhibitor beta-DADF
ATIC complex crystallized in monoclinic space group P2(1), a = 56.48 A, b = 107.88 A, c = 103.86 A and beta = 91.2°
-
crystallized in a binary complex with methotrexate, single crystal at 96 K to 2.3 A resolution, monoclinic crystals, space group P2(1), with unit-cell dimensions a = 65.17, B = 105.93, c= 103.47 A, beta = 108.27 degrees
-
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
sitting drop vapor diffusion method, co-crystallized in the presence of substrate with BW1540 and BW2315
purified recombinant His-tagged enzyme free or in complex with substrate 5-aminoimidazole-4-carboxamide ribonucleotide, both with adventitiously active site-bound nucleotide inhibitor of the cyclohydrolase activity, X-ray diffraction structure determination and analysis at 2.5 A and 2.2 A resolution, respectively
-
the three-dimensional structure of TM1249 is determined to 1.88 A resolution by molecular replacement
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T116S
-
AICAR transformylase/inosine monophosphate cyclohydrolase 346C>G polymorphism
H256A
K255A
K255R
mutation reduces activity by 76%. Mutation increases the Tm by approximately 3°C
N415A
additional information
H256A
complete loss of activity, mutation lowers the thermostability
K255A
complete loss of activity, mutation lowers the thermostability
N415A
decrease in AICAR transformylase activity as compared with wild-type SlugATIC, indicating it might also play essential role in substrate binding. Increase in the thermostability
N415A
the mutation results in decrease in enzyme activity as compared with wild type enzyme
additional information
targeted deletion of the Cryptococcus neoformans gene ADE16 via biolistic transformation of the type strain H99O. The ade16DELTA mutant obtained is subsequently complemented by introducing a wild-type copy of the gene into Safe Haven 1 to create the ade16DELTA + ADE16 strain
additional information
Cryptococcus neoformans ATCC 208821
-
targeted deletion of the Cryptococcus neoformans gene ADE16 via biolistic transformation of the type strain H99O. The ade16DELTA mutant obtained is subsequently complemented by introducing a wild-type copy of the gene into Safe Haven 1 to create the ade16DELTA + ADE16 strain
-
additional information
Cryptococcus neoformans CBS 10515
-
targeted deletion of the Cryptococcus neoformans gene ADE16 via biolistic transformation of the type strain H99O. The ade16DELTA mutant obtained is subsequently complemented by introducing a wild-type copy of the gene into Safe Haven 1 to create the ade16DELTA + ADE16 strain
-
additional information
Cryptococcus neoformans FGSC 9487
-
targeted deletion of the Cryptococcus neoformans gene ADE16 via biolistic transformation of the type strain H99O. The ade16DELTA mutant obtained is subsequently complemented by introducing a wild-type copy of the gene into Safe Haven 1 to create the ade16DELTA + ADE16 strain
-
additional information
-
targeted deletion of the Cryptococcus neoformans gene ADE16 via biolistic transformation of the type strain H99O. The ade16DELTA mutant obtained is subsequently complemented by introducing a wild-type copy of the gene into Safe Haven 1 to create the ade16DELTA + ADE16 strain
-
additional information
-
several site directed mutants created with mutations in the inosine monophosphate cyclohydrolase domain of the enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
1 h, enzyme retains 30% of its AICAR transformylase activity
6
1 h, enzyme retains 60% of its AICAR transformylase activity
6 - 10
the enzyme retains stable at pH 7.0-10.0 with more than 80% activity remaining after 1 h incubation. The enzyme retains 60% of its activity at pH 6.0, but there is a sharp decline in the enzyme activity thereafter at lower pH
6.5 - 10
1. quite stable over a broad pH range from 6.5 to 10
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
the enzyme retains stable at 10-40°C with more than 80% activity remaining after 1 h incubation
42.1
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C
44.7
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C
45
10 min, the bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC) is stable at lower temperatures and both the activities start declining after 45°C
46.9
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C
additional information
effects of ligand binding, susbtrates and inhibitors, on Tms of the recombinant enzyme, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
much less stable during storage in maleate buffer than in Tris or phosphate solutions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C, if the solution of purified enzyme are stored for 3 or 4 months, a requirement for a specific formyl donor can then be shown
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CM-Sepharose column chromatography, DEAE-Sepharose column chromatography, octyl Sepharose column chromatography, and Superdex S200 gel filtration
Ni-NTA agarose resin column chromatography and Superdex 200 gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography and gel filtration
recombinant N-terminally His6-tagged MtbATIC in Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant N-terminally His6-tagged PurH from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration
-
recombinant protein using His-tag
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATICcDNA cloned into a pET28a vector and transformed into Escherichia coli BL21.DE3 for overexpression
-
cloned and expressed
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21.DE3 as His-tag fusion protein
expression of N-terminally His6-tagged MtbATIC in Escherichia coli strain BL21(DE3)
-
gene ADE16, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) pLysS
gene purH, DNA and amino acid sequence analysis and comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
gene purH, expression of N-terminally His6-tagged PurH in Escherichia coli strain Rosetta (DE3)
-
into the plasmid pMH4 for expression in the Escherichia coli strain GeneHogs
-
recombinant enzyme expression of human enzyme in CHO cells also expressing the alpha- and beta-subunits of the folate receptor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high glucose up-regulates the expression and activity of the enzyme and increases the levels of reactive oxygen species and methylglyoxal-derived advanced glycation end products. Overexpression of the enzyme (atic-1) decreases the lifespan and head motility and increases neuronal damage under both standard and high glucose conditions
microRNA-145-5p suppresses cell proliferation, migration, and invasion in upper tract urothelial carcinoma by targeting 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Transfection of the BFTC-909 cell line with miR-145-5p mimics leads to suppressing effects of miR-145-5p on ATIC expression and cell proliferation, migration, and invasion, miR-145-5p downregulates ATIC protein expression. ATIC is a direct target of miR-145-5p in UTUC cells. ATIC knockdown suppresses UTUC cell proliferation, migration, and invasion
there is approximately 2.7fold increased enzyme expression at 5 days of high glucose (13 mM) compared with standard conditions (5 mM)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
drug development
medicine
diagnostics
enzyme variants are used to predict methotrexate response in juvenile idiopathic arthritis, overview
diagnostics
ATIC correlates with a poor prognosis in patients with upper tract urothelial carcinoma (UTUC). ATIC may be a valuable predictor of prognosis and a potential therapeutic target for UTUC
drug development
the enzyme is an important drug target
drug development
important structural difference between human and parasite ATIC enzymes can potentially be exploited to design compounds for fungus-specific ATIC inhibition
drug development
Cryptococcus neoformans ATCC 208821
-
important structural difference between human and parasite ATIC enzymes can potentially be exploited to design compounds for fungus-specific ATIC inhibition
-
drug development
Cryptococcus neoformans CBS 10515
-
important structural difference between human and parasite ATIC enzymes can potentially be exploited to design compounds for fungus-specific ATIC inhibition
-
drug development
Cryptococcus neoformans FGSC 9487
-
important structural difference between human and parasite ATIC enzymes can potentially be exploited to design compounds for fungus-specific ATIC inhibition
-
drug development
-
important structural difference between human and parasite ATIC enzymes can potentially be exploited to design compounds for fungus-specific ATIC inhibition
-
medicine
-
target for development of inhibitors with potential use as chemotherapeutic agents
medicine
target for development of inhibitors with potential use as chemotherapeutic agents
medicine
-
target for development of inhibitors with potential use as chemotherapeutic agents
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Szabados, E.; Hindmarsh, E.J.; Phillips, L.; Duggleby, R.G.; Christopherson, R.I.
5-Aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase from human CCRF-CEM leukemia cells: purification, pH dependence and inhibitors
Biochemistry
33
14237-14245
1994
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens
brenda
Rayl, E.A.; Moroson, B.A.; Beardsley, G.P.
The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping
J. Biol. Chem.
271
2225-2233
1996
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens (P31939), Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Hartman, S.C.; Buchanan, J.M.
Biosynthesis of the purines. XXVI. The Identification of the formyl donors of the transformylation reactions
J. Biol. Chem.
234
1812-1816
1959
Gallus sp.
brenda
Patrick, T.W.; Crosbie, G.W.
Specificity of 4-aminoimidazole-5-carboxamide ribotide transformylase of Escherichia coli
Biochem. J.
124
31-32
1971
Escherichia coli
brenda
Iwai, K.; Fujisawa, Y.; Suzuki, N.
The accumulation of 5'-phosphoribosyl-5amino-4-imidazolecarboxamide in folate-deficient pea seedlings and the enzymatic reaction in which the compound is involved
Agric. Biol. Chem.
36
398-408
1972
Allium cepa, Columba sp., Daucus carota, Escherichia coli, Gallus sp., Petroselinum crispum, Lathyrus oleraceus, Spinacia oleracea, Trifolium sp.
-
brenda
Baggott, J.E.; Krumdieck, C.L.
Folylpoly-gamma-glutamates as cosubstrates of 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carboxamide formyltransferase
Biochemistry
18
1037-1041
1979
Gallus sp.
-
brenda
Mueller, W.T.; Benkovic, S.J.
On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase from chicken liver
Biochemistry
20
337-344
1981
Gallus sp., Mus musculus
brenda
Smith, G.K.; Mueller, T.; Benkovic, P.A.; Benkovic, S.J.
On the cofactor specificity of glycinamide ribonucleotide and 5-aminoimidazole-4-carboxamide ribonucleotide transformylase from chicken liver
Biochemistry
20
1241-1245
1981
Gallus sp.
brenda
Baggott, J.E.; Vaughn, W.H.; Hudson, B.B.
Inhibition of 5-aminoimidazole-4-carboxamide ribotide transformylase, adenosine deaminase and 5'-adenylate deaminase by polyglutamates of methotrexate and oxidized folates and by 5-aminoimidazole-4-carboxamide riboside and ribotide
Biochem. J.
236
193-200
1986
Gallus sp., Mus musculus
brenda
Ha, T.; Morgan, S.L.; Vaughn, W.H; Eto, I.; Baggott, J.E.
Detection of inhibition of 5-aminoimidazole-4-carboxamide ribotide transformylase by thioinosinic acid and azathioprine by a new colorimetric assay
Biochem. J.
272
339-342
1990
Gallus sp., Homo sapiens, Mus musculus
brenda
Boger, D.L.; Haynes, N.E.; Warren, M.S.; Gooljarsingh, L.T.; Ramcharan, J.; Kitos, P.A.; Benkovic, S.J.
Functionalized analogues of 5,8,10-trideazafolate as potential inhibitors of GAR Tfase or AICAR Tfase
Bioorg. Med. Chem.
5
1831-1838
1997
Gallus sp.
brenda
Sugita, T.; Aya, H.; Ueno, M.; Ishizuka, T.; Kawashima, K.
Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase
J. Biochem.
122
309-313
1997
Bacillus subtilis, Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Reyes, V.M.; Greasley, S.E.; Stura, E.A.; Beardsley, G.P.; Wilson, I.A.
Crystallization and preliminary crystallographic investigations of avian 5-aminoimidazole-4-carboxamide ribonucleotide transformylase-inosine monophosphate cyclohydrolase expressed in Escherichia coli
Acta Crystallogr. Sect. D
56
1051-1054
2000
Gallus sp.
-
brenda
Wall, M.; Shim, J.H.; Benkovic, S.J.
Human AICAR transformylase: Role of the 4-Carboxamide of AICAR in binding and catalysis
Biochemistry
39
11303-11311
2000
Escherichia coli, Homo sapiens
brenda
Shim, J.H.; Wall, M.; Benkovic, S.J.; Diaz, N.; Suarez, D.; Merz, K.M., Jr.
Evaluation of the catalytic mechanism of AICAR transformylase by pH-dependent kinetics, mutagenesis, and quantum chemical calculations
J. Am. Chem. Soc.
123
4687-4696
2001
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Vergis, J.M.; Bulock, K.G.; Fleming, K.G.; Beardsley, G.P.
Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity
J. Biol. Chem.
276
7727-7733
2001
Gallus sp., Homo sapiens, Saccharomyces cerevisiae
brenda
Bulock, K.G.; Beardsley, G.P.; Anderson, K.S.
The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase): A surprising lack of substrate channeling
J. Biol. Chem.
277
22168-22174
2002
Gallus sp., Homo sapiens
brenda
Wolan, D.W.; Greasley, S.E.; Beardsley, G.P.; Wilson, I.A.
Structural insights into the avian AICAR transformylase mechanism
Biochemistry
41
15505-15513
2002
Gallus sp., Homo sapiens
brenda
Cheong, C.G.; Wolan, D.W.; Greasley, S.E.; Horton, P.A.; Beardsley, G.P.; Wilson, I.A.
Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates
J. Biol. Chem.
279
18034-18045
2004
Homo sapiens (P31939), Homo sapiens
brenda
Wolan, D.W.; Greasley, S.E.; Wall, M.J.; Benkovic, S.J.; Wilson, I.A.
Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor beta-DADF identifies the folate binding site
Biochemistry
42
10904-10914
2003
Gallus gallus (P31335)
brenda
Vergis, J.M.; Beardsley, G.P.
Catalytic mechanism of the cyclohydrolase activity of human aminoimidazole carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase
Biochemistry
43
1184-1192
2004
Homo sapiens, aves
brenda
Capps, K.J.; Humiston, J.; Dominique, R.; Hwang, I.; Boger, D.L.
Discovery of AICAR Tfase inhibitors that disrupt requisite enzyme dimerization
Bioorg. Med. Chem. Lett.
15
2840-2844
2005
Homo sapiens
brenda
Xu, L.; Li, C.; Olson, A.J.; Wilson, I.A.
Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide transformylase in complex with a novel non-folate inhibitor identified by virtual ligand screening
J. Biol. Chem.
279
50555-50565
2004
Gallus gallus (P31335), Homo sapiens (P31939)
brenda
Li, C.; Xu, L.; Wolan, D.W.; Wilson, I.A.; Olson, A.J.
Virtual screening of human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase against the NCI diversity set by use of AutoDock to identify novel nonfolate inhibitors
J. Med. Chem.
47
6681-6690
2004
Homo sapiens (P31939), Homo sapiens
brenda
Gellekink, H.; Blom, H.J.; den Heijer, M.
Associations of common polymorphisms in the thymidylate synthase, reduced folate carrier and 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase genes with folate and homocysteine levels and venous thrombosis
Clin. Chem. Lab. Med.
45
471-476
2007
Homo sapiens
brenda
Axelrod, H.L.; McMullan, D.; Krishna, S.S.; Miller, M.D.; Elsliger, M.; Abdubek, P.; Ambing, E.; Astakhova, T.; Carlton, D.; Chiu, H.; Clayton, T.; Duan, L.; Feuerhelm, J.; Grzechnik, S.K.; Hale, J.; Han, G.W.; Haugen, J.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Koesema, E.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Oommachen, S.; Paulsen, J.; Quijano, K.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Weekes, D.; White, A.; Wolf, G.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon. A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 ANG. resolution
Proteins Struct. Funct. Bioinform.
71
1042-1049
2008
Thermotoga maritima
brenda
Boccalatte, F.E.; Voena, C.; Riganti, C.; Bosia, A.; DAmico, L.; Riera, L.; Cheng, M.; Ruggeri, B.; Jensen, O.N.; Goss, V.L.; Lee, K.; Nardone, J.; Rush, J.; Polakiewicz, R.D.; Comb, M.J.; Chiarle, R.; Inghirami, G.
The enzymatic activity of 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase is enhanced by NPM-ALK: new insights in ALK-mediated pathogenesis and the treatment of ALCL
Blood
113
2776-2790
2009
Homo sapiens (P31939)
brenda
McGuire, J.J.; Haile, W.H.
Metabolism-blocked antifolates as potential anti-rheumatoid arthritis agents: 4-amino-4-deoxy-5,8,10-trideazapteroyl-D,L-4-methyleneglutamic acid (CH-1504) and its analogs
Biochem. Pharmacol.
77
1161-1172
2009
Homo sapiens
brenda
Deng, Y.; Zhou, X.; Kugel Desmoulin, S.; Wu, J.; Cherian, C.; Hou, Z.; Matherly, L.H.; Gangjee, A.
Synthesis and biological activity of a novel series of 6-substituted thieno[2,3-d]pyrimidine antifolate inhibitors of purine biosynthesis with selectivity for high affinity folate receptors over the reduced folate carrier and proton-coupled folate transpo
J. Med. Chem.
52
2940-2951
2009
Homo sapiens
brenda
Qiu, X.; Yuan, Y.; Gao, Y.
Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli
Acta Crystallogr. Sect. F
67
1590-1594
2011
Escherichia coli
brenda
Baggott, J.E.; Tamura, T.
Evidence for the hypothesis that 10-formyldihydrofolate is the in vivo substrate for aminoimidazolecarboxamide ribotide transformylase
Exp. Biol. Med. (Maywood)
235
271-277
2010
Homo sapiens, Rattus norvegicus
brenda
Le Nours, J.; Bulloch, E.M.; Zhang, Z.; Greenwood, D.R.; Middleditch, M.J.; Dickson, J.M.; Baker, E.N.
Structural analyses of a purine biosynthetic enzyme from Mycobacterium tuberculosis reveal a novel bound nucleotide
J. Biol. Chem.
286
40706-40716
2011
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Liu, Y.; Zhang, C.; Zhang, H.; Li, M.; Yuan, J.; Zhang, Y.; Zhou, J.; Guo, H.; Zhao, L.; Du, Y.; Wang, L.; Ren, L.
Synthesis and antitumor activity of a novel series of 6-substituted pyrrolo[2,3-d]pyrimidines as potential nonclassical antifolates targeting both thymidylate and purine nucleotide biosynthesis
Eur. J. Med. Chem.
93
142-155
2015
Homo sapiens
brenda
Mitchell-Ryan, S.; Wang, Y.; Raghavan, S.; Ravindra, M.P.; Hales, E.; Orr, S.; Cherian, C.; Hou, Z.; Matherly, L.H.; Gangjee, A.
Discovery of 5-substituted pyrrolo[2,3-d]pyrimidine antifolates as dual-acting inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthesis: Implications of inhibiting 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase to AMPK activation and anti-tumor activity
J. Med. Chem.
56
10016-10032
2013
Homo sapiens
brenda
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
J. Med. Chem.
58
1479-1493
2015
Homo sapiens (P31939), Homo sapiens
brenda
Boutchueng-Djidjou, M.; Collard-Simard, G.; Fortier, S.; Hebert, S.S.; Kelly, I.; Landry, C.R.; Faure, R.L.
The last enzyme of the de novo purine synthesis pathway 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC) plays a central role in insulin signaling and the Golgi/endosomes protein network
Mol. Cell. Proteomics
14
1079-1092
2015
Homo sapiens (P31939), Rattus norvegicus (Q6IN16)
brenda
Pastore, S.; Stocco, G.; Moressa, V.; Zandona, L.; Favretto, D.; Malusa, N.; Decorti, G.; Lepore, L.; Ventura, A.
5-Aminoimidazole-4-carboxamide ribonucleotide-transformylase and inosine-triphosphate-pyrophosphatase genes variants predict remission rate during methotrexate therapy in patients with juvenile idiopathic arthritis
Rheumatol. Int.
35
619-627
2015
Homo sapiens (P31939), Homo sapiens
brenda
Witkowska, D.; Cox, H.L.; Hall, T.C.; Wildsmith, G.C.; Machin, D.C.; Webb, M.E.
Analysis of substrate binding in individual active sites of bifunctional human ATIC
Biochim. Biophys. Acta
1866
254-263
2018
Homo sapiens
brenda
Davis, B.W.; Aumiller, W.M.; Hashemian, N.; An, S.; Armaou, A.; Keating, C.D.
Colocalization and sequential enzyme activity in aqueous biphasic systems experiments and modeling
Biophys. J.
109
2182-2194
2015
Homo sapiens
brenda
Liu, Y.; Li, M.; Zhang, H.; Yuan, J.; Zhang, C.; Zhang, K.; Guo, H.; Zhao, L.; Du, Y.; Wang, L.; Ren, L.
Design, synthesis and biological evaluation of 6-substituted pyrrolo[2,3-d]pyrimidines as dual inhibitors of TS and AICARFTase and as potential antitumor agents
Eur. J. Med. Chem.
115
245-256
2016
Homo sapiens
brenda
Xing, R.; Zhang, H.; Yuan, J.; Zhang, K.; Li, L.; Guo, H.; Zhao, L.; Zhang, C.; Li, S.; Gao, T.; Liu, Y.; Wang, L.
Novel 6-substituted benzoyl and non-benzoyl straight chain pyrrolo[2,3-d]pyrimidines as potential antitumor agents with multitargeted inhibition of TS, GARFTase and AICARFTase
Eur. J. Med. Chem.
139
531-541
2017
Homo sapiens
brenda
Verma, P.; Kar, B.; Varshney, R.; Roy, P.; Sharma, A.
Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis
FEBS J.
284
4233-4261
2017
Staphylococcus lugdunensis, Staphylococcus lugdunensis (A0A133Q8U5)
brenda
Markandeyan, D.; Kannaiyan, S.; Suresh, S.; Nimmakayala, R.; Ilamurugan, R.; Santhalingam, K.; Paul, B.
Virtual screening of phytochemicals for methotrexate like dihydrofolate reductase and aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase inhibitory property using Molegro virtual docker
Int. J. Pharm. Pharm. Sci.
8
83-87
2016
Homo sapiens (P31939)
-
brenda
Riedinger, C.; Mendler, M.; Schlotterer, A.; Fleming, T.; Okun, J.; Hammes, H.P.; Herzig, S.; Nawroth, P.P.
High-glucose toxicity is mediated by AICAR-transformylase/IMP cyclohydrolase and mitigated by AMP-activated protein kinase in Caenorhabditis elegans
J. Biol. Chem.
293
4845-4859
2018
Caenorhabditis elegans, Caenorhabditis elegans (Q95QQ4)
brenda
Fales, K.R.; Njoroge, F.G.; Brooks, H.B.; Thibodeaux, S.; Torrado, A.; Si, C.; Toth, J.L.; Mc Cowan, J.R.; Roth, K.D.; Thrasher, K.J.; Frimpong, K.; Lee, M.R.; Dally, R.D.; Shepherd, T.A.; Durham, T.B.; Margolis, B.J.; Wu, Z.; Wang, Y.; Atwell, S.; Wang, J.; Hui, Y.H.; Meier, T.I.; Konicek, S.A.; Geeganage, S.
Discovery of N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), a potent and selective nonclassical antifolate aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT) inhibitor
J. Med. Chem.
60
9599-9616
2017
Homo sapiens (P31939)
brenda
Sah, S.; Shah, R.; Govindan, A.; Varada, R.; Rex, K.; Varshney, U.
Utilisation of 10-formyldihydrofolate as substrate by dihydrofolate reductase (DHFR) and 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) tranformylase/IMP cyclohydrolase (PurH) in Escherichia coli
Microbiology
164
982-991
2018
Escherichia coli, Escherichia coli (P15639), Escherichia coli K12 (P15639)
brenda
Lonare, S.; Rode, S.; Verma, P.; Verma, S.; Kaur, H.; Alam, M.S.; Wangmo, P.; Kumar, P.; Roy, P.; Sharma, A.K.
Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) bifunctional enzyme from Candidatus Liberibacer asiaticus
Biochim. Biophys. Acta
1872
141015
2024
Candidatus Liberibacter asiaticus (C6XFI4), Candidatus Liberibacter asiaticus psy62 (C6XFI4)
brenda
Wallace-Povirk, A.; Tong, N.; Wong-Roushar, J.; OConnor, C.; Zhou, X.; Hou, Z.; Bao, X.; Garcia, G.E.; Li, J.; Kim, S.; Dann, C.E.; Matherly, L.H.; Gangjee, A.
Discovery of 6-substituted thieno[2,3-d]pyrimidine analogs as dual inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthesis in folate receptor expressing human tumors
Bioorg. Med. Chem.
37
116093
2021
Homo sapiens (P31939)
brenda
Wizrah, M.S.I.; Chua, S.M.H.; Luo, Z.; Manik, M.K.; Pan, M.; Whyte, J.M.L.; Robertson, A.A.B.; Kappler, U.; Kobe, B.; Fraser, J.A.
AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans
J. Biol. Chem.
298
102453
2022
Cryptococcus neoformans (J9VJP1), Cryptococcus neoformans ATCC 208821 (J9VJP1), Cryptococcus neoformans CBS 10515 (J9VJP1), Cryptococcus neoformans FGSC 9487 (J9VJP1), Cryptococcus neoformans H99O (J9VJP1)
brenda
Luo, H.L.; Lee, Y.C.; Chang, Y.L.; Hsu, W.C.; Wu, Y.T.; Jhan, J.H.; Lin, H.H.; Wu, Y.R.; Ke, H.L.; Liu, H.Y.
MicroRNA-145-5p suppresses cell proliferation, migration, and invasion in upper tract urothelial carcinoma by targeting 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
J. Cell. Biochem.
124
1324-1345
2023
Homo sapiens (P31939)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.2.3)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
