3.5.1.19: nicotinamidase
This is an abbreviated version!
For detailed information about nicotinamidase, go to the full flat file.
Word Map on EC 3.5.1.19
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3.5.1.19
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mycobacterium
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tuberculosis
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pyrazinamide
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pyrazinoic
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pza-resistant
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bactec
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pyrazinamide-resistant
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sir2-dependent
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kansasii
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wayne
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sir2-mediated
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pza-susceptible
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analysis
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drug development
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medicine
- 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
Reaction
Synonyms
AS87_01735, ASAC_0847, NAAA, NA_As0847, NIC, nicotinamidase, nicotinamidase PNC-1, nicotinamidase Pnc1p, nicotinamidase PncA, nicotinamidase/pyrazinamidase, nicotinamidase/pyrazinamidase PncA, nicotinamide amidase, nicotinamide deaminase, Nicotine deamidase, OiNIC, PNC-1, Pnc1, Pnc1p, PNC2, PncA, polygenomic nicotinamidase, PolyNic, pyrazinamidase, PZAase, PZAse, SpNic, TTHA0328, UbNic, YNDase
ECTree
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Metals Ions
Metals Ions on EC 3.5.1.19 - nicotinamidase
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Co2+
Fe2+
Mg2+
Mn2+
Zn2+
additional information
Co2+
addition of Co2+ after metal removement results in 13% activity
Fe2+
the enzyme contains Fe2+ (0.77 mol per mol of protein). 1.6fold activation by 5 mM Fe2+
Fe2+
addition of Fe2+ after metal removement results in 13% activity
Fe2+
the enzyme contains a Fe2+ ion in its metal binding site, which is coordinated by an aspartate (D67) and three histidine residues (H69, H75 and H86)
Fe2+
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the conserved specific metal ion binding includes one aspartate (D67) and two histidines (H69 and H86)
Mn2+
addition of Mn2+ after metal removement results in 27% activity
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activates, best cation, the active site Cys159 is located at the N-terminus of a6 at one side of the active site with the Zn2+ ion positioned on the other side. The metal ion is bound tightly in the AbPncA active site
Zn2+
presence of Zn2+ in the active center of the enzyme in a molecular ratio of 1:1 of protein to metal ion
Zn2+
contains tightly bound zinc. Addition of 2 mM ZnCl2 fails to increase the activity of the wild type enzyme
Zn2+
contains zinc, highest level of activity in the presence of Zn2+
additional information
the enzyme contains 0.235 mM of Zn2+ in 0.242 mM protein, while it only contains 0.0032 mM of Fe2+ and 0.00077 mM Mn2+
additional information
addition of Fe3+ or Ni2+ after metal removement results in no detectable activity
additional information
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addition of Fe3+ or Ni2+ after metal removement results in no detectable activity