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Information on EC 1.17.1.8 - 4-hydroxy-tetrahydrodipicolinate reductase and Organism(s) Thermotoga maritima and UniProt Accession Q9X1K8

for references in articles please use BRENDA:EC1.17.1.8
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IUBMB Comments
The substrate of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate , and the enzyme was classified accordingly as EC 1.3.1.26, dihydrodipicolinate reductase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual substrate of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate, and that its activity includes a dehydration step , and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate reductase. However, the identity of the substrate is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all .
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Thermotoga maritima
UNIPROT: Q9X1K8
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
dihydrodipicolinate reductase, dhdpr, mrsa-dhdpr, dihydrodipicolinic acid reductase, abdhdpr, 4-hydroxy-tetrahydrodipicolinate reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrodipicolinic acid reductase
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reductase, dihydrodipicolinate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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SYSTEMATIC NAME
IUBMB Comments
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NAD(P)+ 4-oxidoreductase
The substrate of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate [1], and the enzyme was classified accordingly as EC 1.3.1.26, dihydrodipicolinate reductase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual substrate of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate, and that its activity includes a dehydration step [2], and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate reductase. However, the identity of the substrate is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9055-46-3
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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
2,3-dihydrodipicolinate + NAD(P)H
2,3,4,5-tetrahydrodipicolinate + NAD(P)+
show the reaction diagram
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-
?
2,3-dihydrodipicolinate + NADH + H+
2,3,4,5-tetrahydrodipicolinate + NAD+ + H2O
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
the enzyme has a greater affinity for NADPH than for NADH
NADPH
the enzyme has a greater affinity for NADPH than for NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dihydrodipicolinate
the enzyme is inhibited by high concentrations of 2,3-dihydrodipicolinate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0076 - 0.013
2,3-dihydrodipicolinate
0.0018 - 0.0025
NADH
0.0006 - 0.0021
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.1 - 19
2,3-dihydrodipicolinate
0.093 - 0.49
NADH
2.6 - 17
NADPH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0051 - 0.0081
NADH
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
x-ray crystallography
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 95
the enzyme is stable for up to 48 h at 80°C, the melting temperature of DHDPR is at 95.7°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Trap column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL-1 Blue cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pearce, F.G.; Sprissler, C.; Gerrard, J.A.
Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics
J. Biochem.
143
617-623
2008
Thermotoga maritima (Q9X1K8), Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 (Q9X1K8)
Manually annotated by BRENDA team