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Literature summary for 1.4.3.21 extracted from

  • Lee, H.I.; Kim, Y.M.; Ro, Y.T.
    Purification and characterization of a copper-containing amine oxidase from Mycobacterium sp. strain JC1 DSM 3803 grown on benzylamine (2008), J. Biochem., 144, 107-114.
    View publication on PubMed
Search for more literature for 1.4.3.21

Inhibitors

Inhibitors Comment Organism Structure
isoniazid 0.2 mM, 42% inhibition of dimeric enzyme, 39% inhibition of tetrameric enzyme Mycobacterium sp.
KCl 100 mM, 88% inhibition of dimeric and tetrameric enzyme Mycobacterium sp.
additional information no effect: DTT or EDTA at 1 mM, 1,4-diamino-2-butanone, sodium azide or KCN Mycobacterium sp.
NaCl 100 mM, 88% inhibition of dimeric and tetrameric enzyme Mycobacterium sp.
o-phenylenediamine 0.2 mM, 33% inhibition of dimeric enzyme, 26% inhibition of tetrameric enzyme Mycobacterium sp.
Semicarbazide 0.2 mM, 49% inhibition of dimeric enzyme, 45% inhibition of tetrameric enzyme Mycobacterium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0045
-
 benzylamine dimeric enzyme Mycobacterium sp.
0.005
-
 benzylamine tetrameric enzyme Mycobacterium sp.

Metals/Ions

Metals/Ions Comment Organism Structure
copper the purified enzyme contains 2.39 mol of copper per mol of subunit Mycobacterium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
 2 * 75000, SDS-PAGE Mycobacterium sp.
75000
-
 4 * 75000, SDS-PAGE Mycobacterium sp.
150000
-
 dimer, gel filtration Mycobacterium sp.
300000
-
 tetramer, gel filtration Mycobacterium sp.

Organism

Organism UniProt Comment Textmining
Mycobacterium sp.
-
-
-
Mycobacterium sp. DSM 3803 / JC1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium sp.

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:benzylamine-grown cell
-
 Mycobacterium sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1
-
 tetrameric enzyme Mycobacterium sp.
6.7
-
 dimeric enzyme Mycobacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzylamine + H2O + O2 best oxidized substrate Mycobacterium sp. benzaldehyde + NH3 + H2O2
-
 ?
benzylamine + H2O + O2 best oxidized substrate Mycobacterium sp. DSM 3803 / JC1 benzaldehyde + NH3 + H2O2
-
 ?
histamine + H2O + O2
-
 Mycobacterium sp. (imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
 ?
histamine + H2O + O2
-
 Mycobacterium sp. DSM 3803 / JC1 (imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
 ?
tyramine + H2O + O2
-
 Mycobacterium sp. 4-hydroxyphenylethanal + NH3 + H2O2
-
 ?
tyramine + H2O + O2
-
 Mycobacterium sp. DSM 3803 / JC1 4-hydroxyphenylethanal + NH3 + H2O2
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 75000, SDS-PAGE Mycobacterium sp.
tetramer 4 * 75000, SDS-PAGE Mycobacterium sp.

Synonyms

Synonyms Comment Organism
semicarbazide-sensitive amine oxidase
-
 Mycobacterium sp.
SSAO
-
 Mycobacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 specific activities of dimeric and tetrameric enzyme form in Tris buffer at pH 7.0 is about 6fold lower than those in phosphate buffer at same pH Mycobacterium sp.

Cofactor

Cofactor Comment Organism Structure
additional information no evidences of topaquinone cofactor involvement Mycobacterium sp.