4.1.1.45: aminocarboxymuconate-semialdehyde decarboxylase

This is an abbreviated version!
For detailed information about aminocarboxymuconate-semialdehyde decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.45

Reaction

2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
=
2-aminomuconate semialdehyde
+
CO2

Synonyms

Decarboxylase, aminocarboxymuconate semialdehyde, Picolinic acid carboxylase, Picolinic acid decarboxylase, alpha-Amino-beta-carboxymuconate-epsilon-semialdehade decarboxylase, alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde beta-decarboxylase, Amino-carboxymuconate-semialdehyde decarboxylase, Picolinic decarboxylase, ACMSD, 3-(3-oxoprop-2-enyl)-2-aminobut-2-endioate carboxy-lyase, alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase, ACMSDase, 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase, NbaD enzyme, ACMSD I, ACMS decarboxylase, 2-amino 3-carboxymuconate 6-semialdehyde decarboxylase, alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase, alpha-amino beta-carboxymuconate epsilon-semialdehyde decarboxylase, hACMSD, picolinic carboxylase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.45 aminocarboxymuconate-semialdehyde decarboxylase

Engineering

Engineering on EC 4.1.1.45 - aminocarboxymuconate-semialdehyde decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H8A
-
activity decreases by about 50%
H6A
-
activity decreases by about 82%
H228A
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
R51K
-
catalytically inactive
R51A
-
catalytically inactive
H177A
H9E
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
H228E
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
D294E
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
R239A
-
catalytically inactive
H228Y
the mutant contains iron rather than zinc and is catalytically inactive
H228G
the mutant contains iron rather than zinc and is catalytically inactive
R239K
-
catalytically inactive