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4.1.1.20: diaminopimelate decarboxylase

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

Word Map on EC 4.1.1.20

Reaction

meso-2,6-diaminoheptanedioate
=
L-lysine
 +
CO2

Synonyms

At3g14390, At5g11880, Ba-DAPDC, BAS1329, CgDAPDC, Cgl1180, DAP decarboxylase, DAP decarboxylase 1, DAP decarboxylase 2, DAP-decarboxylase, DAPDC, DAPDC 1, DAPDC 2, DDC, Decarboxylase, diaminopimelate, diaminopimelate decarboxylase, diaminopimelate decarboxylase 1, diaminopimelate decarboxylase 2, Diaminopimelic acid decarboxylase, Ec-DAPDC, LysA, LYSA1, LYSA2, meso-DAP decarboxylase, meso-diaminopimelate decarboxylase, meso-diaminopimelic acid decarboxylase, Mt-DAPDC, Vc-DAPDC

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.20 diaminopimelate decarboxylase

Engineering

Engineering on EC 4.1.1.20 - diaminopimelate decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E375A
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
M408A
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
R302A
site-directed mutagenesis of a substrate binding site residue, the mutant shows about 65% reduced activity compared to wild-type
R343A
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
Y347A
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
Y412A
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
M408A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
-
R302A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
site-directed mutagenesis of a substrate binding site residue, the mutant shows about 65% reduced activity compared to wild-type
-
R343A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
-
Y347A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
-
Y412A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
site-directed mutagenesis of a substrate binding site residue, the mutant is almost completely inactive
-
I148A
mutant shows 2% catalytic efficiency compared to the wild type enzyme
I148D
mutant shows 0.2% catalytic efficiency compared to the wild type enzyme
I148F
mutant shows 15% catalytic efficiency compared to the wild type enzyme
I148G
mutant shows 0.5% catalytic efficiency compared to the wild type enzyme
I148K
mutant shows 2% catalytic efficiency compared to the wild type enzyme
I148L
mutant shows 28% catalytic efficiency compared to the wild type enzyme
N381A
site-directed mutagenesis, the mutant shows impaired dimerization and is significantly attenuated in catalytic activity
R385A
site-directed mutagenesis, the mutant shows impaired dimerization and is significantly attenuated in catalytic activity
N381A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
site-directed mutagenesis, the mutant shows impaired dimerization and is significantly attenuated in catalytic activity
-
R385A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
site-directed mutagenesis, the mutant shows impaired dimerization and is significantly attenuated in catalytic activity
-