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Information on EC 1.1.1.205 - IMP dehydrogenase and Organism(s) Leishmania donovani and UniProt Accession P21620

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     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.205 IMP dehydrogenase
IUBMB Comments
The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.
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This record set is specific for:
Leishmania donovani
UNIPROT: P21620
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Word Map
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The taxonomic range for the selected organisms is: Leishmania donovani
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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IMP
+
NAD+
+
H2O
=
XMP
+
NADH
+
H+
+
+
=
+
+
Synonyms
impdh, imp dehydrogenase, inosine monophosphate dehydrogenase, impdh2, impdh1, inosine 5'-monophosphate dehydrogenase, inosine-5'-monophosphate dehydrogenase, impdh ii, imp dh, inosinate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inosine 5'-monophosphate dehydrogenase
-
dehydrogenase, inosinate
-
-
-
-
IMP dehydrogenase
-
-
-
-
IMP oxidoreductase
-
-
-
-
IMPD
-
-
-
-
IMPDH
inosinate dehydrogenase
-
-
-
-
inosine 5'-monophosphate dehydrogenase
-
-
-
-
inosine monophosphate dehydrogenase
inosine monophosphate oxidoreductase
-
-
-
-
inosine-5'-phosphate dehydrogenase
-
-
-
-
inosinic acid dehydrogenase
-
-
-
-
Raspberry protein
-
-
-
-
SOI12
-
-
-
-
Superoxide-inducible protein 12
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
IMP:NAD+ oxidoreductase
The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-93-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
show the reaction diagram
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
show the reaction diagram
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mycophenolic acid
-
Mycophenolic acid
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
inosine 5'-phosphate
-
pH 7.5, 25°C
0.39
NAD+
-
pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
GMP
-
pH 7.5, 25°C
0.0000002 - 0.000025
Mycophenolic acid
0.026
XMP
-
pH 7.5, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
is a key enzyme in the biosynthesis of purine nucleotides
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IMDH_LEIDO
514
0
55552
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
204000
-
gel filtration
55000
-
4 * 55000, SDS-PAGE
55560
-
calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
4 * 55000, SDS-PAGE
additional information
-
IMPDH associates tightly with glycosomal protein sorting receptor PEX5
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified protein remains active for more than 18 months
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
genes from: Leishmania donovani
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilson, K.; Collart, F.R.; Huberman, E.; Stringer, J.R.; Ullman, B.
Amplification and molecular cloning of the IMP dehydrogenase gene of Leishmania donovani
J. Biol. Chem.
266
1665-1671
1991
Leishmania donovani, Leishmania donovani MPA100
Manually annotated by BRENDA team
Dobie, F.; Berg, A.; Boitz, J.M.; Jardim, A.
Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani
Mol. Biochem. Parasitol.
152
11-21
2007
Leishmania donovani
Manually annotated by BRENDA team
Hedstrom, L.
IMP dehydrogenase: Structure, mechanism, and inhibition
Chem. Rev.
109
2903-2928
2009
Klebsiella aerogenes, Candida albicans, Cricetulus griseus, Escherichia coli, Eimeria tenella, Staphylococcus aureus, Plasmodium falciparum, Pyrococcus horikoshii, Toxoplasma gondii, no activity in Giardia lamblia, no activity in Trichomonas vaginalis, Streptococcus pyogenes (P0C0H6), Homo sapiens (P12268), Homo sapiens (P20839), Leishmania donovani (P21620), Borreliella burgdorferi (P49058), Tritrichomonas suis (P50097), Trypanosoma brucei (P50098), Pneumocystis carinii (Q12658), Cryptosporidium parvum (Q8T6T2)
Manually annotated by BRENDA team
Shu, Q.; Nair, V.
Inosine monophosphate dehydrogenase (IMPDH) as a target in drug discovery
Med. Res. Rev.
28
219-232
2008
Borreliella burgdorferi, Cricetulus griseus, Escherichia coli, Leishmania donovani, Mycobacterium tuberculosis, Mus musculus, Rattus norvegicus, Streptococcus pyogenes, Thermotoga maritima, Tritrichomonas suis, Pyrococcus horikoshii OT3, Homo sapiens (P12268), Homo sapiens (P20839)
Manually annotated by BRENDA team