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
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4.1.1.20
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aspartokinase
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decarboxylases
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dihydrodipicolinate
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sphaericus
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nutrition
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plp-dependent
- 4.1.1.20
- aspartokinase
- decarboxylases
- dihydrodipicolinate
- sphaericus
- nutrition
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plp-dependent
Reaction
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
4.1.1.20 diaminopimelate decarboxylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.1.1.20 - diaminopimelate decarboxylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DD-2,6-diaminoheptanedioate
L-lysine + CO2
DD-2,6-diaminoheptanedioate is a reasonable substrate for DAPDC but with an about 100fold lower kcat/Km value than DL-DAP
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?
diaminopimelate
L-lysine + CO2
a step in the lysine biosynthetic pathway, overview
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-
?
diaminopimelate
L-lysine + CO2
a step in the lysine biosynthetic pathway, overview
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-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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-
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?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
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final step in L-lysine biosynthesis
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?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
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last step in L-lysine biosynthesis
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?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
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?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
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?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
commercial meso-2,6-diaminoheptanedioate is a mixture of 50% DL-2,6-diaminoheptanedioate, 25% DD-2,6-diaminoheptanedioate and 25% LL-2,6-diaminoheptanedioate
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-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
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-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
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-
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?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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ir
additional information
?
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A0A1S0QVH4
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
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-
?
additional information
?
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-
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
A0A1S0QVH4
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
-
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
A0A1S0QVH4
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
A0A1S0QVH4
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
the position of the alpha15 helix in CgDAPDC and the residues located on the helix are crucial for determining the substrate specificities of the amino acid decarboxylases. Substrate binding mode of enzyme CgDAPDC, substrate binding site involves residues Arg302, Arg343, Tyr347, Glu375, Tyr404, Met408, and Tyr412
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?
additional information
?
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the position of the alpha15 helix in CgDAPDC and the residues located on the helix are crucial for determining the substrate specificities of the amino acid decarboxylases. Substrate binding mode of enzyme CgDAPDC, substrate binding site involves residues Arg302, Arg343, Tyr347, Glu375, Tyr404, Met408, and Tyr412
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-
?
additional information
?
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Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
the position of the alpha15 helix in CgDAPDC and the residues located on the helix are crucial for determining the substrate specificities of the amino acid decarboxylases. Substrate binding mode of enzyme CgDAPDC, substrate binding site involves residues Arg302, Arg343, Tyr347, Glu375, Tyr404, Met408, and Tyr412
-
-
?
additional information
?
-
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
-
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
-
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
Escherichia coli K-12 / MG1655
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
Escherichia coli K-12 / MG1655
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
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-
the reaction catalyzed by diaminopimelate decarboxylase on D stereocenters could be a concerted, backside electrophilic substitution reaction with simultaneous CO2 loss from Calpha and proton donation to the backside of Calpha from Lys72
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?
additional information
?
-
the reaction catalyzed by diaminopimelate decarboxylase on D stereocenters could be a concerted, backside electrophilic substitution reaction with simultaneous CO2 loss from Calpha and proton donation to the backside of Calpha from Lys72
-
-
?
additional information
?
-
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
-
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
-
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
Mycobacterium tuberculosis ATCC 25618 / H37Rv
optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
Mycobacterium tuberculosis ATCC 25618 / H37Rv
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
the reaction catalyzed by diaminopimelate decarboxylase on D stereocenters could be a concerted, backside electrophilic substitution reaction with simultaneous CO2 loss from Calpha and proton donation to the backside of Calpha from Lys72
-
-
?
additional information
?
-
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer
-
-
?
