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Information on EC 1.1.1.205 - IMP dehydrogenase and Organism(s) Borreliella burgdorferi and UniProt Accession P49058

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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:
Borreliella burgdorferi
UNIPROT: P49058
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The taxonomic range for the selected organisms is: Borreliella burgdorferi
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
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL 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
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1H-naphtho[2,3-d]imidazol-2-ylmethyl 4-aminobenzoate
-
-
2-[(3-ethyl-4-oxo-3,4-dihydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(4-methoxyphenyl)acetamide
-
-
3-(1H-naphtho[2,3-d]imidazol-2-yl)propyl 4-aminobenzoate
-
-
GMP
-
competitive with respect to IMP
methyl 3-methyl-2-oxo-1,2-dihydroquinoline-4-carboxylate
-
-
Mycophenolic acid
N-(4-methoxyphenyl)-2-(3-methyl-4-oxo-3,4-dihydrophthalazin-1-yl)acetamide
-
-
N-(4-methoxyphenyl)-2-[2-(1,3-thiazol-4-yl)-1H-benzimidazol-1-yl]acetamide
-
-
N-(naphthalen-2-yl)-2-[2-(pyridin-2-yl)-5,6-dihydro-1H-benzimidazol-1-yl]acetamide
-
-
NAD+
-
substrate inhibition at high concentration
P1-(thiazofurin-5'-yl)-P2-(adenosyl-5'-yl)-alpha,beta-methylene diphosphate
-
-
thiazole-4-carboxamide adenine dinucleotide
-
uncompetitive with respect to IMP and NAD
xanthosine 5'-phosphate
-
competitive with respect to IMP
additional information
-
overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029
inosine 5'-phosphate
-
in the presence of 25 mM K+
1.1
NAD+
-
in the presence of 25 mM K+
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
inosine 5'-phosphate
-
in the presence of 25 mM K+
additional information
additional information
-
overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
Mycophenolic acid
-
-
0.0016
P1-(thiazofurin-5'-yl)-P2-(adenosyl-5'-yl)-alpha,beta-methylene diphosphate
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00022
1H-naphtho[2,3-d]imidazol-2-ylmethyl 4-aminobenzoate
Borreliella burgdorferi
-
pH 8.0, 25°C
0.0008
2-[(3-ethyl-4-oxo-3,4-dihydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(4-methoxyphenyl)acetamide
Borreliella burgdorferi
-
pH 8.0, 25°C
0.0009
3-(1H-naphtho[2,3-d]imidazol-2-yl)propyl 4-aminobenzoate
Borreliella burgdorferi
-
pH 8.0, 25°C
0.0009
methyl 3-methyl-2-oxo-1,2-dihydroquinoline-4-carboxylate
Borreliella burgdorferi
-
pH 8.0, 25°C
0.0017
N-(4-methoxyphenyl)-2-(3-methyl-4-oxo-3,4-dihydrophthalazin-1-yl)acetamide
Borreliella burgdorferi
-
pH 8.0, 25°C
0.0006
N-(4-methoxyphenyl)-2-[2-(1,3-thiazol-4-yl)-1H-benzimidazol-1-yl]acetamide
Borreliella burgdorferi
-
pH 8.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
is a key enzyme in the biosynthesis of purine nucleotides
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43640
-
calculated from amino acid composition
44000
additional information
-
equilibrium sedimentation results suggest monomeric, dimeric and tetrameric forms and higher order aggregates
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.4 A resolution
-
in complex with sulfate, at 2.4 A resolution
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
95% homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, X.; Cahoon, M.; Rosa, P.; Hedstrom, L.
Expression, purification, and characterization of inosine 5'-monophosphate dehydrogenase from Borrelia burgdorferi
J. Biol. Chem.
35
21977-21981
1997
Borreliella burgdorferi
Manually annotated by BRENDA team
Goldstein, B.M.; Colby, T.D.
IMP dehydrogenase: Structural aspects of inhibitor binding
Curr. Med. Chem.
6
519-536
1999
Borreliella burgdorferi, Cricetulus griseus, Homo sapiens, Streptococcus pyogenes, Tritrichomonas suis
Manually annotated by BRENDA team
Hedstrom, L.
IMP dehydrogenase: Mechanism of action and inhibition
Curr. Med. Chem.
6
545-560
1999
Borreliella burgdorferi, Escherichia coli, Eimeria tenella, Homo sapiens, Rattus norvegicus, Tritrichomonas suis
Manually annotated by BRENDA team
Pimkin, M.; Markham, G.
Inosine 5-monophosphate dehydrogenase
Adv. Enzymol. Relat. Areas Mol. Biol.
76
1-53
2009
Klebsiella aerogenes, Borreliella burgdorferi, Saccharomyces cerevisiae, Candida albicans, Cricetulus griseus, Cryptosporidium parvum, Escherichia coli, Homo sapiens, Mus musculus, Streptococcus pyogenes, Tritrichomonas suis
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
Gollapalli, D.R.; Macpherson, I.S.; Liechti, G.; Gorla, S.K.; Goldberg, J.B.; Hedstrom, L.
Structural determinants of inhibitor selectivity in prokaryotic IMP dehydrogenases
Chem. Biol.
17
1084-1091
2010
Borreliella burgdorferi, Escherichia coli, Helicobacter pylori, Streptococcus pyogenes
Manually annotated by BRENDA team