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Literature summary extracted from

  • Lee, Y.; Nelson, M.; Snell, E.
    Enzymes of vitamin B6 degradation. Purification and properties of isopyridoxal dehydrogenase and 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid dehydrogenase (1986), J. Biol. Chem., 261, 15106-15111 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.416 4-deoxyisopyridoxal competitive Arthrobacter sp. Cr-7
1.1.1.416 5-pyridoxic acid competitive Arthrobacter sp. Cr-7
1.1.1.416 DTNB 0.005 mM, 50% loss of activity after 1 h Arthrobacter sp. Cr-7
1.1.1.416 HgCl2 0.02 mM, 67% loss of activity after 1 h Arthrobacter sp. Cr-7
1.1.1.416 N-ethylmaleimide 2.5 mM, 71% loss of activity after 1 h Arthrobacter sp. Cr-7
1.1.1.416 NADH noncompetitive Arthrobacter sp. Cr-7
1.1.1.416 PCMB 0.005 mM, 75% loss of activity after 1 h Arthrobacter sp. Cr-7
1.1.1.416 Thionicotinamide adenine dinucleotide noncompetitive Arthrobacter sp. Cr-7
1.2.1.102 4-deoxyisopyridoxal competitive Arthrobacter sp. Cr-7
1.2.1.102 5-pyridoxic acid competitive Arthrobacter sp. Cr-7
1.2.1.102 DTNB 0.005 mM, 50% loss of activity after 1 h Arthrobacter sp. Cr-7
1.2.1.102 HgCl2 0.02 mM, 67% loss of activity after 1 h Arthrobacter sp. Cr-7
1.2.1.102 N-ethylmaleimide 2.5 mM, 71% loss of activity after 1 h Arthrobacter sp. Cr-7
1.2.1.102 NADH noncompetitive Arthrobacter sp. Cr-7
1.2.1.102 PCMB 0.005 mM, 75% loss of activity after 1 h Arthrobacter sp. Cr-7
1.2.1.102 Thionicotinamide adenine dinucleotide noncompetitive Arthrobacter sp. Cr-7

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.416 0.04
-
 NAD+ pH 8.0, 25°C Arthrobacter sp. Cr-7
1.1.1.416 0.04
-
 Isopyridoxal pH 8.0, 25°C Arthrobacter sp. Cr-7
1.2.1.100 0.025
-
 NAD+ pH 8.0, temperature not specified in the publication Pseudomonas sp. MA-1
1.2.1.100 0.1
-
 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate pH 8.0, temperature not specified in the publication Pseudomonas sp. MA-1
1.2.1.102 0.04
-
 NAD+ pH 8.0, 25°C Arthrobacter sp. Cr-7
1.2.1.102 0.04
-
 Isopyridoxal pH 8.0, 25°C Arthrobacter sp. Cr-7

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.416 242000
-
 gel filtration Arthrobacter sp. Cr-7
1.1.99.42 65000
-
-
 Pseudomonas sp. MA-1
1.2.1.100 65000
-
-
 Pseudomonas sp. MA-1
1.2.1.102 242000
-
 gel filtration Arthrobacter sp. Cr-7

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.416 isopyridoxal + NAD+ Arthrobacter sp. Cr-7 the enzyme participates in the degradation of pyridoxine 5-pyridoxolactone + NADH + H+
-
 ?
1.2.1.102 isopyridoxal + NAD+ + H2O Arthrobacter sp. Cr-7 the enzyme participates in the degradation of pyridoxine 5-pyridoxate + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.416 Arthrobacter sp. Cr-7
-
-
-
1.1.99.42 Pseudomonas sp. MA-1
-
-
-
1.2.1.100 Pseudomonas sp. MA-1
-
-
-
1.2.1.102 Arthrobacter sp. Cr-7
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.416
-
 Arthrobacter sp. Cr-7
1.2.1.102
-
 Arthrobacter sp. Cr-7

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.416 isopyridoxal + NAD+ the enzyme participates in the degradation of pyridoxine Arthrobacter sp. Cr-7 5-pyridoxolactone + NADH + H+
-
 ?
1.1.1.416 isopyridoxal + NAD+ the enzyme also catalyses the activity of EC 1.2.1.102, isopyridoxal dehydrogenase (5-pyridoxate-forming) Arthrobacter sp. Cr-7 5-pyridoxolactone + NADH + H+
-
 ?
1.1.99.42 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NADH + H+
-
 Pseudomonas sp. MA-1 4-pyridoxate + NAD+
-
 ?
1.1.99.42 additional information enzyme catalyzes with equal facility both the oxidation of formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid by NAD+ to 3-hydroxy-2-methylpyridine-4,5-dicarboxylic acid, i.e. reaction of EC 1.2.1.100, and the reduction of formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid by NADH to 4-pyridoxic acid. No oxidation of 4-pyridoxic acid is observed Pseudomonas sp. MA-1 ?
-
 ?
1.2.1.100 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
-
 Pseudomonas sp. MA-1 3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
-
 ?
1.2.1.100 additional information enzyme catalyzes with equal facility both the oxidation of formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid by NAD+ to 3-hydroxy-2-methylpyridine-4,5-dicarboxylic acid and the reduction of formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid by NADH to 4-pyridoxic acid, i.e. reaction of 4-pyridoxic acid dehydrogenase. No oxidation of 4-pyridoxic acid is observed Pseudomonas sp. MA-1 ?
-
 ?
1.2.1.102 isopyridoxal + NAD+ + H2O the enzyme participates in the degradation of pyridoxine Arthrobacter sp. Cr-7 5-pyridoxate + NADH + H+
-
 ?
1.2.1.102 isopyridoxal + NAD+ + H2O the enzyme also catalyses the activity of EC 1.1.1.416, isopyridoxal dehydrogenase (5-pyridoxolactone-forming) Arthrobacter sp. Cr-7 5-pyridoxate + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.416 homotetramer 4 * 60000, SDS-PAGE Arthrobacter sp. Cr-7
1.1.99.42 dimer
-
 Pseudomonas sp. MA-1
1.2.1.100 dimer
-
 Pseudomonas sp. MA-1
1.2.1.102 homotetramer 4 * 60000, SDS-PAGE Arthrobacter sp. Cr-7

Synonyms

EC Number Synonyms Comment Organism
1.1.1.416 isopyridoxal dehydrogenase
-
 Arthrobacter sp. Cr-7
1.2.1.102 isopyridoxal dehydrogenase
-
 Arthrobacter sp. Cr-7

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.416 10
-
 Isopyridoxal pH 8.0, 25°C Arthrobacter sp. Cr-7
1.2.1.100 400 670 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate pH 8.0, temperature not specified in the publication Pseudomonas sp. MA-1
1.2.1.102 10
-
 Isopyridoxal pH 8.0, 25°C Arthrobacter sp. Cr-7

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.416 8 8.6
-
 Arthrobacter sp. Cr-7
1.1.99.42 7.8 8.5
-
 Pseudomonas sp. MA-1
1.2.1.100 7.8 8.5
-
 Pseudomonas sp. MA-1
1.2.1.102 8 8.6
-
 Arthrobacter sp. Cr-7

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.416 NAD+ no activity with NADP+ or thionicotinamide adenine dinucleotide Arthrobacter sp. Cr-7
1.2.1.102 NAD+ no activity with NADP+ or thionicotinamide adenine dinucleotide Arthrobacter sp. Cr-7

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.416 0.00065
-
 4-deoxyisopyridoxal pH 8.0, 25°C Arthrobacter sp. Cr-7
1.1.1.416 0.13
-
 Thionicotinamide adenine dinucleotide pH 8.0, 25°C Arthrobacter sp. Cr-7
1.1.1.416 0.25
-
 NADH pH 8.0, 25°C Arthrobacter sp. Cr-7
1.1.1.416 0.7
-
 5-pyridoxic acid pH 8.0, 25°C Arthrobacter sp. Cr-7
1.2.1.102 0.00065
-
 4-deoxyisopyridoxal pH 8.0, 25°C Arthrobacter sp. Cr-7
1.2.1.102 0.13
-
 Thionicotinamide adenine dinucleotide pH 8.0, 25°C Arthrobacter sp. Cr-7
1.2.1.102 0.25
-
 NADH pH 8.0, 25°C Arthrobacter sp. Cr-7
1.2.1.102 0.7
-
 5-pyridoxic acid pH 8.0, 25°C Arthrobacter sp. Cr-7

Expression

EC Number Organism Comment Expression
1.1.1.416 Arthrobacter sp. Cr-7 the enzyme is induced in response to growth of the organisms on pyridoxine up
1.1.99.42 Pseudomonas sp. MA-1 expression is induced in response to growth on pyridoxine up
1.2.1.100 Pseudomonas sp. MA-1 expression is induced in response to growth on pyridoxine up
1.2.1.102 Arthrobacter sp. Cr-7 the enzyme is induced in response to growth of the organisms on pyridoxine up

General Information

EC Number General Information Comment Organism
1.1.1.416 metabolism the enzyme participates in the degradation of pyridoxine Arthrobacter sp. Cr-7
1.2.1.102 metabolism the enzyme participates in the degradation of pyridoxine Arthrobacter sp. Cr-7