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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

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

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