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Information on EC 3.5.1.19 - nicotinamidase and Organism(s) Mycobacterium tuberculosis and UniProt Accession I6XD65
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3.5.1.19 nicotinamidaseSpecify your search results
Word Map
- 3.5.1.19
- mycobacterium
- tuberculosis
- pyrazinamide
-
pyrazinoic
-
pza-resistant
-
bactec
-
pyrazinamide-resistant
-
sir2-dependent
- kansasii
-
wayne
-
sir2-mediated
-
pza-susceptible
- analysis
- drug development
- medicine
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pzase, nicotinamidase, pnc1p, pnc-1, pzaase, nicotinamidase/pyrazinamidase, yndase, as87_01735, nicotinamidase pnc-1, nicotinamidase pnca, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nicotinamide amidase
-
-
-
-
nicotinamide deaminase
-
-
-
-
Nicotine deamidase
-
-
-
-
YNDase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
nicotinamide amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9033-32-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
nicotinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
0.014
nicotinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
0.016
Pyrazinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
0.3
Pyrazinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
nicotinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
3.1
nicotinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
0.1
Pyrazinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
3.8
Pyrazinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
37
nicotinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
220
nicotinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
6.2
Pyrazinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
13
Pyrazinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00029
3-pyridine carboxaldehyde
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
0.1
pyridine-3-carbonitrile
-
Ki about 0.1 mM, wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview
additional information
-
structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20890
-
determined by analytical ultracentrifugation and mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
2 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, structural model of enzyme homodimer, overview
monomer
1 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H57D
-
the mutant has reduced Mn2+ content and shows a 6fold and 38fold decrease in kcat value for nicotinamide and pyrazinamide, respectively
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pncA, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in Escherichia coli strain BL21(DE3)pLysS
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
enzyme is involved in the activation of the antituberculosis drug pyrazinamide
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boshoff, H.I.; Mizrahi, V.
Purification, gene cloning, targeted knockout, overexpression, and biochemical characterization of the major pyrazinamidase from Mycobacterium smegmatis
J. Bacteriol.
180
5809-5814
1998
Mycobacterium tuberculosis, Mycolicibacterium smegmatis
Raynaud, C.; Etienne, G.; Peyron, P.; Laneelle, M.A.; Daffe, M.
Extracellular enzyme activities potentially involved in the pathogenicity of Mycobacterium tuberculosis
Microbiology
144
577-587
1998
Mycobacterium tuberculosis, Mycobacterium tuberculosis variant bovis, Mycolicibacterium fortuitum, Mycobacterium kansasii, Mycolicibacterium phlei
-
Zhang, H.; Deng, J.Y.; Bi, L.J.; Zhou, Y.F.; Zhang, Z.P.; Zhang, C.G.; Zhang, Y.; Zhang, X.E.
Characterization of Mycobacterium tuberculosis nicotinamidase/pyrazinamidase
FEBS J.
275
753-762
2008
Mycobacterium tuberculosis
Seiner, D.R.; Hegde, S.S.; Blanchard, J.S.
Kinetics and inhibition of nicotinamidase from Mycobacterium tuberculosis
Biochemistry
49
9613-9619
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Rueda, D.; Sheen, P.; Gilman, R.H.; Bueno, C.; Santos, M.; Pando-Robles, V.; Batista, C.V.; Zimic, M.
Nicotinamidase/pyrazinamidase of Mycobacterium tuberculosis forms homo-dimers stabilized by disulfide bonds
Tuberculosis
94
644-648
2014
Mycobacterium tuberculosis (I6XD65), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (I6XD65)
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