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Information on EC 1.4.1.16 - diaminopimelate dehydrogenase and Organism(s) Ureibacillus thermosphaericus and UniProt Accession G1UII1

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This record set is specific for:
Ureibacillus thermosphaericus
UNIPROT: G1UII1 not found.
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Word Map
The taxonomic range for the selected organisms is: Ureibacillus thermosphaericus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
meso-diaminopimelate dehydrogenase, meso-dapdh, diaminopimelate dehydrogenase, meso-2,6-diaminopimelate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
meso-diaminopimelate dehydrogenase
-
NADP+-dependent meso-diaminopimelate dehydrogenase
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meso-alpha,epsilon-diaminopimelate dehydrogenase
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-
-
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meso-diaminopimelate dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
meso-2,6-diaminoheptanedioate:NADP+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
60894-21-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-DELTA1-tetrahydrodipicolinate + NH4+ + NADPH
meso-2,6-diaminoheptanedioate + NADP+
show the reaction diagram
-
-
-
?
meso-2,6-diaminoheptanedioate + H2O + NADP+
L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+
show the reaction diagram
meso-2,6-diaminoheptanedioate + NADP+
L-DELTA1-tetrahydrodipicolinate + NH4+ + NADPH
show the reaction diagram
-
-
-
?
meso-2,6-diaminoheptanedioate + H2O + NADP+
L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
meso-2,6-diaminoheptanedioate + H2O + NADP+
L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+
show the reaction diagram
meso-2,6-diaminoheptanedioate + H2O + NADP+
L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
meso-diaminopimelate dehydrogenase catalyzes the NAD(P)-dependent oxidative deamination of meso-diaminopimelate stereoselectively acting on the D-configuration of meso-diaminopimelate. The enzyme is highly selective for meso-diaminopimelate as the electron donor, and NADP+ but not NAD+ can serve as the electron acceptor
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MnSO4
slight activation, mutant enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
complete inhibition at 5 mM
4-chloromercuribenzoate
complete inhibition at 0.1 mM
HgCl2
complete inhibition at 0.1 mM
N-ethylmaleimide
strong inhibition at 1 mM
Ni2+
strong inhibition at 1 mM
thioglycolate
complete inhibition at 5 mM
Zn2+
strong inhibition at 1 mM
4-chloromercuribenzoate
-
complete inhibition at 0.1 mM
Cu2+
-
strong inhibition at 1 mM
HgCl2
-
complete inhibition at 0.1 mM
L-cysteine
-
strong inhibition at 5 mM
Thioglycollate
-
strong inhibition at 5 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
L-DELTA1-tetrahydrodipicolinate
pH 8.5, 30°C
-
1.9
meso-2,6-diaminoheptanedioate
pH 10, 30°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50.6
L-DELTA1-tetrahydrodipicolinate
pH 8.5, 30°C
-
123.3
meso-2,6-diaminoheptanedioate
pH 10, 30°C
347.7
NH4+
pH 8.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
194.6
L-DELTA1-tetrahydrodipicolinate
pH 8.5, 30°C
-
64.9
meso-2,6-diaminoheptanedioate
pH 10, 30°C
53.4
NH4+
pH 8.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.28
-
purified enzyme, pH 7.2, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.5
reductive amination
11.5
oxidative deamination
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
substrate specificity of mut-DAADH Q154L/D158G/T173I/R199M/H249N , overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DAPDH_URETH
326
0
36010
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
2 * 40000 SDS-PAGE
80000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
homodimer
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2 * 40000 SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo form and in complex with NADP+ and N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid, sitting drop vapor diffusion method, using 1.9 M ammonium sulfate,0.1 M Tris-HCl pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q154L/D158G/T173I/R199M/H249N
construction of a thermostable, NADP+-dependent D-amino acid dehydrogenase (DAADH) from the meso-diaminopimelate dehydrogenase of strain A1 by introducing five point mutations into amino acid residues located in the active site. In the presence of NADP+, the mutant enzyme catalyzes the oxidative deamination of several D-amino acids, including D-cyclohexylalanine, D-isoleucine, and D-2-aminooctanoate, but not of meso-diaminopimelate. The corresponding 2-oxo acids are aminated in the presence of NADPH and ammonia in the reverse reaction, mutant substrate specificity, overview. The mutant enzyme is also more thermostable than its parental meso-diaminopimelate dehydrogenase
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
purified enzyme, 30 min, 50°C, fully stable
723913
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
purified mutant enzyme, 30 min, pH 7.2, fully stable, half-liife is 80 min
60
-
purified enzyme, 30 min, pH 7.2, fully stable
65
-
purified enzyme, 30 min, pH 7.2, loss of 50% activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni+-charged chelating Sepharose column chromatography and Toyopearl butyl-650M column chromatography
recombinant wild-type enzyme and mutant Q154L/D158G/T173I/R199M/H249N from Escherichia coli strain Rosetta (DE3) by heat treatment and chelating affinity chromatograhy
recombinant enzyme from Escherichia coli strain Rosetta (DE3) by heat treatment and affinity chromatography, native enzyme 47fold to homogeneity by ammonium sulfate fractionation, and hydrophobic interaction and anion exchange chromatography, followed by preparative slab PAGE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
gene ddh, expression of wild-type enzyme and mutant Q154L/D158G/T173I/R199M/H249N in Escherichia coli strain Rosetta (DE3)
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain Rosetta (DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akita, H.; Fujino, Y.; Doi, K.; Ohshima, T.
Highly stable meso-diaminopimelate dehydrogenase from an Ureibacillus thermosphaericus strain A1 isolated from a Japanese compost: purification, characterization and sequencing
AMB Express
1
43
2011
Ureibacillus thermosphaericus, Ureibacillus thermosphaericus A1
Manually annotated by BRENDA team
Akita, H.; Doi, K.; Kawarabayasi, Y.; Ohshima, T.
Creation of a thermostable NADP+-dependent D-amino acid dehydrogenase from Ureibacillus thermosphaericus strain A1 meso-diaminopimelate dehydrogenase by site-directed mutagenesis
Biotechnol. Lett.
34
1693-1699
2012
Ureibacillus thermosphaericus (G1UII1), Ureibacillus thermosphaericus, Ureibacillus thermosphaericus A1 (G1UII1)
Manually annotated by BRENDA team
Akita, H.; Seto, T.; Ohshima, T.; Sakuraba, H.
Structural insight into the thermostable NADP+-dependent meso-diaminopimelate dehydrogenase from Ureibacillus thermosphaericus
Acta Crystallogr. Sect. D
71
1136-1146
2015
Ureibacillus thermosphaericus (G1UII1), Ureibacillus thermosphaericus
Manually annotated by BRENDA team
Xu, J.Z.; Ruan, H.Z.; Liu, L.M.; Wang, L.P.; Zhang, W.G.
Overexpression of thermostable meso-diaminopimelate dehydrogenase to redirect diaminopimelate pathway for increasing L-lysine production in Escherichia coli
Sci. Rep.
9
2423
2019
Acetivibrio thermocellus (A3DDX7), Acetivibrio thermocellus ATCC 27405 (A3DDX7), Bacteroides fragilis (Q64PZ8), Bacteroides fragilis YCH46 (Q64PZ8), Corynebacterium glutamicum (P04964), Corynebacterium glutamicum ATCC 13032 (P04964), Lysinibacillus sphaericus (Q9KWR0), Symbiobacterium thermophilum (Q67PI3), Ureibacillus thermosphaericus (G1UII1)
Manually annotated by BRENDA team