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Literature summary for 1.17.1.5 extracted from

  • Holcenberg, J.S.; Stadtman, E.R.
    Nicotinic acid metabolism. III. Purification and properties of a nicotinic acid hydroxylase (1969), J. Biol. Chem., 244, 1194-1203.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
arsenate activates less than phosphate Clostridium sp.
methylphosphate activates less than phosphate Clostridium sp.
additional information not activated by high concentrations of citrate, sulfate, or diphosphate Clostridium sp.
phosphate slight activation, half-maximal activation at 50 mM Clostridium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.028
-
NADP+
-
Clostridium sp.
0.11
-
nicotinate
-
Clostridium sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Clostridium sp.
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
300000
-
analytical ultracentrifugation Clostridium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nicotinate + H2O + NADP+ Clostridium sp. first step in the anaerobic decomposition of nicotinate, NADP+ may be the natural, primary electron acceptor 6-hydroxynicotinate + NADPH
-
?

Organism

Organism UniProt Comment Textmining
Clostridium sp.
-
nicotinic acid-fermenting
-

Purification (Commentary)

Purification (Comment) Organism
24fold increase in specific activity Clostridium sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
28.8
-
-
Clostridium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-pyrazinecarboxylate + H2O + NADP+ 30% of the activity with nicotinate Clostridium sp. ?
-
r
additional information not as substrates: nicotinamide, isonicotinate, picolinate, nicotinic acid N-oxide, N-methylnicotinamide, trigonelline, hypoxanthine, not as electron acceptor: NAD+ Clostridium sp. ?
-
?
nicotinate + H2O + NADP+ specific for NADP+, but artificial electron acceptors, i.e. benzyl viologen and 2,3,5-triphenyltetrazolium dyes, can replace NADP+, high substrate specificity with respect to nicotinate, requiring an unsubstituted pyridine or pyrazine ring nitrogen and a carboxyl group meta to the nitrogen Clostridium sp. 6-hydroxynicotinate + NADPH
-
r
nicotinate + H2O + NADP+ equilibrium lies far in direction of 6-hydroxynicotinate formation Clostridium sp. 6-hydroxynicotinate + NADPH
-
r
nicotinate + H2O + NADP+ first step in the anaerobic decomposition of nicotinate, NADP+ may be the natural, primary electron acceptor Clostridium sp. 6-hydroxynicotinate + NADPH
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
hydroxylase activity is more sensitive to heat inactivation than are diaphorase and NADPH-oxidase activities Clostridium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8 phosphate buffer Clostridium sp.
8
-
triethanolamine phosphate buffer Clostridium sp.
8 8.5 triethanolamine buffer Clostridium sp.
8.3 9 Tris buffer or diphosphate buffer Clostridium sp.
8.5
-
dimethylglutarate-phosphate buffer Clostridium sp.

Cofactor

Cofactor Comment Organism Structure
benzyl viologen can replace NADP+ Clostridium sp.
FAD FAD as prosthetic group, 1.5 mol flavin per mol of enzyme Clostridium sp.
additional information NAD+/NADH can not replace NADP+/NADPH Clostridium sp.
additional information enzyme contains 11 mol non-heme iron and 6 mol acid-labile sulfide per mole of enzyme Clostridium sp.
NADP+ specific for NADP+, artificial electron acceptors, i.e. benzyl viologen and 2,3,5-triphenyltetrazolium dyes, can replace NADP+ Clostridium sp.
NADPH NADPH oxidase activity Clostridium sp.