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Literature summary extracted from

  • Barker, H.A.; Kahn, J.M.; Chew, S.
    Enzymes involved in 3,5-diaminohexanoate degradation by Brevibacterium sp. (1980), J. Bacteriol., 143, 1165-1170.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.247 additional information no effect on enzyme activity by 0.5 mM DTNB Brevibacterium sp.
2.3.1.247 phosphate weak inhibition Brevibacterium sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.247 additional information no effect on enzyme activity by Co2+ and Mg2+ at 0.1 mM Brevibacterium sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.247 123000
-
 native enzyme, gel filtration Brevibacterium sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.247 (5S)-5-amino-3-oxohexanoate + acetyl-CoA Brevibacterium sp.
-
 L-3-aminobutanoyl-CoA + acetoacetate
-
 r
2.3.1.247 (5S)-5-amino-3-oxohexanoate + acetyl-CoA Brevibacterium sp. L5
-
 L-3-aminobutanoyl-CoA + acetoacetate
-
 r
4.3.1.14 additional information Brevibacterium sp. enzyme is induced by growth on 3,5-diaminohexanoate ?
-
 ?
4.3.1.14 additional information Brevibacterium sp. L5 enzyme is induced by growth on 3,5-diaminohexanoate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.247 Brevibacterium sp.
-
-
-
2.3.1.247 Brevibacterium sp. L5
-
-
-
4.3.1.14 Brevibacterium sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.247 native soluble enzyme 78fold by ammonium sulfate fractionation and anion exchange chromatography, followed by ultrafiltration and adsorption chromatography Brevibacterium sp.
4.3.1.14 partial Brevibacterium sp.

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.247 culture condition:DL-erythro-3,5-diaminohexanoate-grown cell
-
 Brevibacterium sp.
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.247 0.105
-
 crude enzyme extract, pH 7.0, 25°C Brevibacterium sp.
2.3.1.247 12.5
-
 purified enzyme, pH 7.0, 25°C Brevibacterium sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.247 (5S)-5-amino-3-oxohexanoate + acetyl-CoA
-
 Brevibacterium sp. L-3-aminobutanoyl-CoA + acetoacetate
-
 r
2.3.1.247 (5S)-5-amino-3-oxohexanoate + acetyl-CoA preferred substrate, the substrate is cleaved between C-2 and C-3 to form C-2 and C-4 moieties Brevibacterium sp. L-3-aminobutanoyl-CoA + acetoacetate DL-3-aminobutyryl-CoA and acetoacetate are used in the reverse reaction assay r
2.3.1.247 (5S)-5-amino-3-oxohexanoate + acetyl-CoA
-
 Brevibacterium sp. L5 L-3-aminobutanoyl-CoA + acetoacetate
-
 r
2.3.1.247 (5S)-5-amino-3-oxohexanoate + acetyl-CoA preferred substrate, the substrate is cleaved between C-2 and C-3 to form C-2 and C-4 moieties Brevibacterium sp. L5 L-3-aminobutanoyl-CoA + acetoacetate DL-3-aminobutyryl-CoA and acetoacetate are used in the reverse reaction assay r
4.3.1.14 L-3-Aminobutanoyl-CoA
-
 Brevibacterium sp. Crotonyl-CoA + NH3
-
 ?
4.3.1.14 L-3-Aminobutanoyl-CoA
-
 Brevibacterium sp. L5 Crotonyl-CoA + NH3
-
 ?
4.3.1.14 additional information enzyme is induced by growth on 3,5-diaminohexanoate Brevibacterium sp. ?
-
 ?
4.3.1.14 additional information enzyme is induced by growth on 3,5-diaminohexanoate Brevibacterium sp. L5 ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.247 25
-
 assay at Brevibacterium sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.247 7
-
 forward reaction assay at Brevibacterium sp.
2.3.1.247 8
-
 reverse reaction Brevibacterium sp.

General Information

EC Number General Information Comment Organism
2.3.1.247 metabolism C-1 and C-2 of 3-oxo-5-aminohexanoate are converted mainly to acetoacetate and acetate, whereas C-3 to C-6 are converted mainly to 3-hydroxybutyrate or its coenzyme A thiolester. 3-Aminobutyryl-CoA is then deaminated to form crotonyl-CoA. The enzymes observed in extracts of Brevibacterium sp. can account for the conversion of 3,5-diaminohexanoate to acetyl-CoA, overview Brevibacterium sp.