Information on EC 4.1.1.20 - Diaminopimelate decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
4.1.1.20
-
RECOMMENDED NAME
GeneOntology No.
Diaminopimelate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
meso-2,6-Diaminoheptanedioate = L-lysine + CO2
show the reaction diagram
stereochemistry
-
meso-2,6-Diaminoheptanedioate = L-lysine + CO2
show the reaction diagram
stereochemistry
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-lysine biosynthesis I
-
-
L-lysine biosynthesis II
-
-
L-lysine biosynthesis III
-
-
L-lysine biosynthesis VI
-
-
Lysine biosynthesis
-
-
lysine metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
meso-2,6-diaminoheptanedioate carboxy-lyase (L-lysine-forming)
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
At3g14390
Q949X7
locus name
At5g11880
Q94A94
locus name
DAP decarboxylase
-
-
-
-
DAP decarboxylase 1
Q949X7
-
DAP decarboxylase 2
Q94A94
-
DAP-decarboxylase
-
-
-
-
DAPDC
Q949X7, Q94A94
-
DAPDC
P56129
-
DAPDC
Q6ZG77
-
DAPDC 1
Q949X7
-
DAPDC 2
Q94A94
-
Decarboxylase, diaminopimelate
-
-
-
-
diaminopimelate decarboxylase 1
Q949X7
-
diaminopimelate decarboxylase 2
Q94A94
-
Diaminopimelic acid decarboxylase
-
-
-
-
LysA
Corynebacterium glutamicum ATC21799
-
gene name
-
LYSA1
Q949X7
gene name
LYSA2
Q94A94
gene name
meso-DAP decarboxylase
-
-
meso-DAP decarboxylase
Corynebacterium glutamicum ATC21799
-
-
-
meso-diaminopimelate decarboxylase
-
-
-
-
meso-diaminopimelate decarboxylase
-
-
meso-diaminopimelate decarboxylase
Corynebacterium glutamicum ATC21799
-
-
-
meso-diaminopimelate decarboxylase
P56129
-
CAS REGISTRY NUMBER
COMMENTARY
9024-75-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DAPDC2; gene DAPDC2
SwissProt
Manually annotated by BRENDA team
isoform DAPDC 1
SwissProt
Manually annotated by BRENDA team
isoform DAPDC 2
SwissProt
Manually annotated by BRENDA team
precursor DAPDC1; gene DAPDC1
SwissProt
Manually annotated by BRENDA team
Chlamydomonas sp.
-
-
-
Manually annotated by BRENDA team
Clostridium spp.
-
-
-
Manually annotated by BRENDA team
Corynebacterium glutamicum ATC21799
-
-
-
Manually annotated by BRENDA team
soy bean
-
-
Manually annotated by BRENDA team
duckweed
-
-
Manually annotated by BRENDA team
duckweed
-
-
Manually annotated by BRENDA team
parental strain AS1 and its G49 derivative
-
-
Manually annotated by BRENDA team
tobacco
-
-
Manually annotated by BRENDA team
a single DAPDC gene
SwissProt
Manually annotated by BRENDA team
wheat
-
-
Manually annotated by BRENDA team
bean
-
-
Manually annotated by BRENDA team
corn
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D,D-2,6-diaminoheptanedioate
L-lysine + CO2
show the reaction diagram
-
-
-
-
?
DD-2,6-diaminoheptanedioate
L-lysine + CO2
show the reaction diagram
-
DD-2,6-diaminoheptanedioate is a reasonable substrate for DAPDC but with an about 100fold lower kcat/Km value than DL-DAP
-
-
?
diaminopimelate
L-lysine + CO2
show the reaction diagram
Q949X7, Q94A94
-
-
-
?
diaminopimelate
L-lysine + CO2
show the reaction diagram
Q6ZG77
-
-
-
?
diaminopimelate
L-lysine + CO2
show the reaction diagram
Q949X7, Q94A94
a step in the lysine biosynthetic pathway, overview
-
-
?
diaminopimelate
L-lysine + CO2
show the reaction diagram
Q6ZG77
a step in the lysine biosynthetic pathway, overview
-
-
?
DL-2,6-diaminoheptanedioate
L-lysine + CO2
show the reaction diagram
-
-
-
-
?
Lanthionine
?
show the reaction diagram
-
slowly
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
Chlamydomonas sp.
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
Clostridium spp., Fibrobacter succinogenes
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
P9WIU7
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
P56129
-
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
final step in L-lysine biosynthesis
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
last step in L-lysine biosynthesis
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
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
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
P9WIU7
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
-
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
Corynebacterium glutamicum AS019
-
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
Corynebacterium glutamicum ATC21799
-
-
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
Bacillus megaterium CII 19
-
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
Bacillus megaterium CII 19
-
lysine biosynthesis
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diaminopimelate
L-lysine + CO2
show the reaction diagram
Q949X7, Q94A94
-
-
-
?
diaminopimelate
L-lysine + CO2
show the reaction diagram
Q949X7, Q94A94
a step in the lysine biosynthetic pathway, overview
-
-
?
diaminopimelate
L-lysine + CO2
show the reaction diagram
Q6ZG77
a step in the lysine biosynthetic pathway, overview
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
P9WIU7
-
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
final step in L-lysine biosynthesis
-
?
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
-
last step in L-lysine biosynthesis
-
?
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
-
lysine biosynthesis
-
-
-
meso-2,6-Diaminoheptanedioate
L-Lysine + CO2
show the reaction diagram
P9WIU7
-
-
?
meso-2,6-Diaminoheptanedioate
?
show the reaction diagram
Bacillus megaterium CII 19
-
lysine biosynthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
absolute requirement
pyridoxal 5'-phosphate
-
Km: 0.002 mM
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
Km: 0.0061 mM
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q949X7, Q94A94
; dependent on, the DAPDC1 protein contains a PLP binding consensus site, overview
pyridoxal 5'-phosphate
Q6ZG77
dependent on, the DAPDC1 protein contains a PLP binding consensus site, overview
pyridoxal 5'-phosphate
P56129
-
pyridoxal 5'-phosphate
P9WIU7
-
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
activates
Na+
-
activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,5-Diaminopentane
-
-
1,6-diaminohexane
-
-
1,7-Diaminoheptane
-
-
2,3-Diaminopropionic acid
-
-
Aminooxyacetate
-
-
D,L-alpha-aminoheptanedioate
-
-
D-Lysine
-
-
D-Lysine
-
not
D-Lysine
-
; a small amount of decarboxlation occurs
diaminoheptanedioic acid
-
analogs
glutamic acid
-
-
L,L-2,6-diaminoheptanedioate
-
no detectable amounts of decarboxylation products
L-2,4-diaminobutyrate
-
-
L-2,4-diaminobutyrate
-
-
L-cystine
-
-
L-lysine
-
-
L-lysine
-
involved in sequential feedback inhibition, pH-dependent
L-lysine
-
reversed by diaminoheptanedioate addition
L-lysine
-
; no detectable amounts of decarboxylation products
L-ornithine
-
-
L-S-aminoethylcysteine
-
-
LL-2,6-Diaminoheptanedioate
-
-
mercuribenzoic acid
-
-
n-butylamine
-
-
N-Hydroxydiaminoheptanedioate
-
Ki: 0.91 mM
N-Hydroxydiaminoheptanedioate
-
Ki: 0.71 mM
NH2OH
-
-
p-chloromercuribenzoate
-
-
Penicillamine
-
no effect at 10fold pyridoxal phosphate concentration
meso-2,6-diaminoheptanedioate
-
substrate inhibition
additional information
-
various substrate analogs
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Dimercaptopropan-1-ol
-
activates
2,3-Dimercaptopropan-1-ol
-
activates
D-Lysine
-
activates
dithiothreitol
-
activates
EDTA
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1 - 7
D,D-2,6-diaminoheptanedioate
-
pH 7.8, 25C
0.43
DL-2,6-Diaminoheptanedioate
-
in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication
1.7
meso-2,6-diamininoheptanedioate
-
-
1.7
meso-2,6-diamininoheptanedioate
-
-
0.03
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148L, in 100 mM Tris, pH 8.0
0.1
meso-2,6-diaminoheptanedioate
-
-
0.11
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148F, in 100 mM Tris, pH 8.0
0.166
meso-2,6-diaminoheptanedioate
-
-
0.3
meso-2,6-diaminoheptanedioate
-
-
0.35
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148A, in 100 mM Tris, pH 8.0
0.36
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148G, in 100 mM Tris, pH 8.0; mutant enzyme I148K, in 100 mM Tris, pH 8.0
0.39
meso-2,6-diaminoheptanedioate
P56129
wild type enzyme, in 100 mM Tris, pH 8.0
0.4
meso-2,6-diaminoheptanedioate
-
pH 7.8, 25C
0.72
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148D, in 100 mM Tris, pH 8.0
1
meso-2,6-diaminoheptanedioate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
D,D-2,6-diaminoheptanedioate
-
pH 7.8, 25C
1.8
DD-2,6-diaminoheptanedioate
-
in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication
7.1
DL-2,6-Diaminoheptanedioate
-
in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication
0.07
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148D, in 100 mM Tris, pH 8.0; mutant enzyme I148G, in 100 mM Tris, pH 8.0
0.28
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148K, in 100 mM Tris, pH 8.0
0.33
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148A, in 100 mM Tris, pH 8.0
0.38
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148L, in 100 mM Tris, pH 8.0
0.68
meso-2,6-diaminoheptanedioate
P56129
mutant enzyme I148F, in 100 mM Tris, pH 8.0
7.1
meso-2,6-diaminoheptanedioate
-
in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication; pH 7.8, 25C
15.65
meso-2,6-diaminoheptanedioate
P56129
wild type enzyme, in 100 mM Tris, pH 8.0
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
D,D-2,6-diaminoheptanedioate
-
pH 7.8, 25C
194866
16
DL-2,6-Diaminoheptanedioate
-
in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication
20250
18
meso-2,6-diaminoheptanedioate
-
pH 7.8, 25C
1400
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
1,5-Diaminopentane
-
-
0.0024
1,6-diaminohexane
-
-
0.0025
1,7-Diaminoheptane
-
-
0.13
Adipic acid
-
-
0.089
azelaic acid
-
-
0.21
caproic acid
-
-
26
D-Lysine
-
in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication; pH 7.8, 25C
1.6
L,L-2,6-diaminoheptanedioate
-
pH 7.8, 25C
1.8
L-lysine
-
in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication; pH 7.8, 25C
1.6
LL-2,6-Diaminoheptanedioate
-
in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication
0.91
N-Hydroxydiaminoheptanedioate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
Chlamydomonas sp.
-
-
0.017
-
-
0.046 - 0.058
-
-
0.048
-
-
0.09
-
wild-type strain AS1
0.209
Clostridium spp.
-
-
0.45
-
mutant G49 strain
7
-
recombinant DDC, 37C
9
-
native DDC
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9
-
more than half-maximal activity between 7.5 and pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
enzyme assay at
30
-
enzyme assay at
37
-
enzyme assay at
37
-
enzyme assay at
37
-
enzyme assay at
37
-
enzyme assay at
additional information
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
relative rates of decarboxylation at 25C, 37C, 45C are 0.17 : 1.0 : 1.6
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.54
Q949X7, Q94A94
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q949X7, Q94A94
-
Manually annotated by BRENDA team
Q949X7, Q94A94
-
Manually annotated by BRENDA team
Q949X7, Q94A94
-
Manually annotated by BRENDA team
additional information
Q949X7, Q94A94
DAPDC1 spatial expression pattern in various tissues, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q949X7, Q94A94
the enzyme contains a transit peptide-like sequence at the N-terminus
Manually annotated by BRENDA team
Q6ZG77
the enzyme contains a transit peptide-like sequence at the N-terminus
Manually annotated by BRENDA team
Bacillus megaterium CII 19
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52500
-
gel filtration, recombinant DDC
649192
80000
-
gel filtration
4115
105000
-
gel filtration
4111
189000
-
X-ray scattering
705411
200000
-
-
4110
200000
-
ultracentrifugation
649192
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 50000, mass spectrometry
?
Q6ZG77
x * 53200, about, sequence calculation
?
Q949X7, Q94A94
x * 53600, about, sequence calculation
?
-
x * 47000, estimated from amino acid sequence, x * 50290, recombinant protein, estimated from SDS-PAGE
?
Corynebacterium glutamicum ATC21799
-
x * 47000, estimated from amino acid sequence, x * 50290, recombinant protein, estimated from SDS-PAGE
-
homodimer
-
DAPDC is predominantly dimeric in solution
homodimer
-
DAPDC is predominantly dimeric in solution
-
homotetramer
-
an equilibrium may exist between the dimeric and the tetrameric form, X-ray crystallography
homotetramer
-
an equilibrium may exist between the dimeric and the tetrameric form, X-ray crystallography
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.0 A resolution; to 2.3 A resolution
Q949X7, Q94A94
vapor-diffusion at room temperature, crystals are grown from 0.002 mL DDC solution in 50 mM sodium MES, pH 6.0 and 0.1 mM pyridoxal 5'-phosphate mixed with 0.002 ml well solution consisting of 1.44-1.54 M lithium sulfate, 50 mM MES, pH 6.0, and 0.1 mM pyridoxal 5'-phosphate
-
hanging drop vapour diffusion method, in 100 mM bicine, pH 8.0, and 1.6 M ammonium sulfate, at 4C
P56129
co-crystals of DAPDC and azelaic acid and L-lysine at 2.6 A and 2.0 A resolution, respectively, hanging drop vapor-diffusion, 12% polyethylene glycol 6000, 100 mm Tris-Cl, pH 8.0, 20 mM MgCl2 and 10 mM L-lysine
-
hanging drop vapor diffusion method, using 20-23% (w/v) PEG-MME 5000, 0.1 M MES pH 6.1-6.6, and 60 mM (NH4)2SO4
-
hanging-drop vapour-diffusion method, crystals grown in absence of substrate or cofactor are colourless and appear to contain one homotetramer of LysA in the asymmetric unit
-
vapor-diffusion in hanging drops at 18C, crystals grow within 3-7 days in 0.004 ml hanging-drops containing 0.002 ml of DAPDC at 10 mg/ml and 5 mM lysine, equilibration against 0.5 ml well solution containing 24% polyethylene glycol mono-methylester 5000, 100 mM MES, pH 6.3, and 60 mM ammonium sulfate, crystals diffract to 2.6 A
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
stable for 10 min at pH 6.0-7.5
4115
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, sodium phosphate buffer, pH 6.8, 4 months, about 50% loss of activity
-
2C, sodium phosphate buffer, pH 6.8, several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography
P56129
Ni-NTA column chromatography
-
recombinant DAPDC
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; expression in Escherichia coli
Q949X7, Q94A94
gene DAPDC1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, overview; gene DAPDC2, localization on chromosome V, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, overview
Q949X7, Q94A94
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in FR3T3 and other mammalian cells
-
overexpression in Escherichia coli
-
expressed in Escherichia coli strain BL21 (DE3)
P56129
expression in Escherichia coli
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
gene DAPDC, location on chromosome II, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, overview, functional complementation of lysine biosynthesis-defective Escherichia coli strains in minimal medium
Q6ZG77
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a 2fold increase in L-lysine production is observed after introduction of the cloned LysA gene into Escherichia coli
-
a 2fold increase in L-lysine production is observed after introduction of the cloned LysA gene into Escherichia coli
Corynebacterium glutamicum ATC21799
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I148A
P56129
mutant shows 2% catalytic efficiency compared to the wild type enzyme
I148D
P56129
mutant shows 0.2% catalytic efficiency compared to the wild type enzyme
I148F
P56129
mutant shows 15% catalytic efficiency compared to the wild type enzyme
I148G
P56129
mutant shows 0.5% catalytic efficiency compared to the wild type enzyme
I148K
P56129
mutant shows 2% catalytic efficiency compared to the wild type enzyme
I148L
P56129
mutant shows 28% catalytic efficiency compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
-
lysine complementation of calf nutrition by lysine-overproducing rumen bacteria, considered