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Literature summary extracted from

  • Huo, L.; Liu, F.; Iwaki, H.; Li, T.; Hasegawa, Y.; Liu, A.
    Human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) a structural and mechanistic unveiling (2015), Proteins, 83, 178-187 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.45 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.45 EPR spectroscopic study on the Cu-substituted enzyme and crystal structure in the native catalytically active state at 1.99 A resolution, a substrate analogue-bound form at 2.50 A resolution, and a selected active site mutant form with one of the putative substrate binding residues altered at 2.32 A resolution. Each asymmetric unit contains three pairs of dimers. The substrate analogue does not directly coordinate to the metal ion but is bound to the active site by two arginine residues through noncovalent interactions Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.45 additional information not inhibitory: EDTA, 1,10-phenanthroline or 8-hydroxyquinoline-5-sulfonic acid Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.45 0.0033
-
 2-aminomuconate semialdehyde Cu-substituted enzyme, pH 7.0, temperature not specified in the publication Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.45 additional information the addition of one to ten equivalents of Co2+, Cu2+, Fe2+, or Zn2+ to purified ACMSD does not increase enzyme activity Homo sapiens
4.1.1.45 Zn2+ the activity of ACMSD is proportional to the zinc content of the enzyme Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.45 Homo sapiens Q8TDX5
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.45 0.8
-
 recombinant enzyme, pH 7.0, temperature not specified in the publication Homo sapiens
4.1.1.45 3.54
-
 recombinant enzyme, presence of Zn2+ in expression medium, pH 7.0, temperature not specified in the publication Homo sapiens

Storage Stability

EC Number Storage Stability Organism
4.1.1.45 -78°C, enzyme endures freeze/thaw cycles multiple times without a significant loss of activity Homo sapiens
4.1.1.45 4°C, stable for weeks Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.45 2-aminomuconate semialdehyde + CO2
-
 Homo sapiens 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.45 ACMSD
-
 Homo sapiens
4.1.1.45 alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.45 0.1
-
 2-aminomuconate semialdehyde Cu-substituted enzyme, pH 7.0, temperature not specified in the publication Homo sapiens
4.1.1.45 4.8
-
 2-aminomuconate semialdehyde enzyme with 64.4% zinc ion occupancy, pH 7.0, temperature not specified in the publication Homo sapiens