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Information on EC 1.1.1.28 - D-lactate dehydrogenase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC1.1.1.28
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Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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(R)-lactate
+
NAD+
=
pyruvate
+
NADH
+
H+
+
=
+
+
Synonyms
ldh, d-lactate dehydrogenase, d-ldh, paldh, fermentative lactate dehydrogenase, nad-dependent d-lactate dehydrogenase, d-nldh, ljd-ldh, d-(-)-lactate dehydrogenase, d-ldh1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-(-)-lactate dehydrogenase (NAD)
-
-
-
-
D-lactic acid dehydrogenase
-
-
-
-
D-lactic dehydrogenase
-
-
-
-
D-LDH
D-specific lactic dehydrogenase
-
-
-
-
dehydrogenase, D-lactate
-
-
-
-
Fermentative lactate dehydrogenase
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
LDH
-
-
-
-
Respiratory D-lactate dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
allosteric mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(R)-lactate:NAD+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-36-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
show the reaction diagram
-
-
-
r
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
show the reaction diagram
-
-
-
r
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
show the reaction diagram
-
-
-
r
glyoxylate + NADH + H+
hydroxyacetate + NAD+
show the reaction diagram
-
-
-
r
hydroxypyruvate + NADH + H+
glycerate + NAD+
show the reaction diagram
-
-
-
r
oxaloacetate + NADH + H+
malate + NAD+
show the reaction diagram
-
-
-
r
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
show the reaction diagram
-
-
-
r
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
pyruvate + NADH + H+
(R)-lactate + NAD+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxamate
inhibits the catalytic reaction of PALDH in a mixed--type manner at pH 7.0, but markedly enhances the enzyme reaction at low concentration through canceling of the apparent homotropic cooperativity at pH 8.0
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fructose 1,6-bisphosphate
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.64
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
5.8
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
12
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
4
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
6.8
glyoxylate
pH 7.0, 30°C, recombinant enzyme
3
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
0.019 - 0.035
NADH
1.7
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
7.1
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
0.1 - 1.2
pyruvate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
100
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
160
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
39
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
69
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
880
glyoxylate
pH 7.0, 30°C, recombinant enzyme
420
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
270 - 310
NADH
410
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
18
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
240 - 400
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
27
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
3.2
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
18
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
130
glyoxylate
pH 7.0, 30°C, recombinant enzyme
140
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
7700 - 17000
NADH
230
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
2.6
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
200 - 4000
pyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
44
glyoxylate
pH 7.0, 30°C, recombinant enzyme
19
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
1.8 - 20
pyruvate
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A485HEN2_PSEAI
329
0
35773
TrEMBL
-
A0A485INF9_PSEAI
76
0
8380
TrEMBL
-
A0A485IQV4_PSEAI
92
0
10203
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
recombinant His-tagged enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
4 * 37800, about, sequence calculation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of the apo and ternary complex structures of Fusobacterium nucleatum FnLDH and Escherichia coli EcLDH and Pseudomonas aeruginosa PaLDH. FnLDH and EcLDH exhibit positive cooperativity in substrate binding, and PaLDH shows negatively cooperative substrate binding. The three enzymes consistently form homotetrameric structures with three symmetric axes, the P-, Q-, and R-axes, which allows apo-FnLDH and EcLDH to form wide intersubunit contact surfaces between the opened catalytic domains of the two Q-axis-related subunits in coordination with their asymmetric and distorted quaternary structures. apo-PaLDH possesses a highly symmetrical quaternary structure and partially closed catalytic domains that are favorable for initial substrate binding and forms virtually no intersubunit contact surface between the catalytic domains
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
purified recombinant His-tagged enzyme, 30°C, 1 h, stable at
739841
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57
purified recombinant His-tagged enzyme, pH 5.0, stable up to
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by two different steps of affinity chromatography, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pa0927, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Furukawa, N.; Miyanaga, A.; Togawa, M.; Nakajima, M.; Taguchi, H.
Diverse allosteric and catalytic functions of tetrameric D-lactate dehydrogenases from three Gram-negative bacteria
AMB Express
4
76
2014
Escherichia coli (A0A140N893), Escherichia coli, Fusobacterium nucleatum subsp. nucleatum (Q8RG11), Pseudomonas aeruginosa (Q9I530), Pseudomonas aeruginosa, Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847 (Q8RG11)
Manually annotated by BRENDA team
Furukawa, N.; Miyanaga, A.; Nakajima, M.; Taguchi, H.
Structural basis of sequential allosteric transitions in tetrameric D-lactate dehydrogenases from three Gram-negative bacteria
Biochemistry
57
5388-5406
2018
Escherichia coli (A0A140N893), Escherichia coli, Fusobacterium nucleatum subsp. nucleatum (Q8RG11), Pseudomonas aeruginosa (Q9I530), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I530), Fusobacterium nucleatum subsp. nucleatum DSM 15643 (Q8RG11), Escherichia coli BL21-DE3 (A0A140N893)
Manually annotated by BRENDA team