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Information on EC 1.17.1.8 - 4-hydroxy-tetrahydrodipicolinate reductase and Organism(s) Corynebacterium glutamicum and UniProt Accession P40110
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1.17.1.8 4-hydroxy-tetrahydrodipicolinate reductaseIUBMB 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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Word Map
- 1.17.1.8
- diaminopimelate
- glutamicum
- meso-diaminopimelate
- aspartokinase
- imine
- dhdps
- 2,6-pyridinedicarboxylate
- medicine
-
alpha,beta-unsaturated
-
2'-phosphate
- s-2-aminoethyl-l-cysteine
-
aspartate-semialdehyde
- drug development
- agriculture
The taxonomic range for the selected organisms is: Corynebacterium glutamicum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
dihydrodipicolinate reductase, dhdpr, mrsa-dhdpr, dihydrodipicolinic acid reductase, abdhdpr, 4-hydroxy-tetrahydrodipicolinate reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dihydrodipicolinic acid reductase
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-
-
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reductase, dihydrodipicolinate
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
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oxidation
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -
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
9055-46-3
-
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
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
involved in L-lysine biosynthesis
-
-
?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
the enzyme utilizes both NADH and NADPH as cofactors
-
-
?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
the enzyme utilizes both NADH and NADPH as cofactors
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-
?
2,3-dihydrodipicolinate + NAD(P)H
2,3,4,5-tetrahydrodipicolinate + NAD(P)+
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-
-
-
?
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
the enzyme is involved in L-lysine biosynthesis
-
-
?
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
it is proposed that the the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme
-
-
?
NATURAL SUBSTRATE
NATURAL 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
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
the enzyme is involved in L-lysine biosynthesis
-
-
?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
involved in L-lysine biosynthesis
-
-
?
2,3-dihydrodipicolinate + NAD(P)H
2,3,4,5-tetrahydrodipicolinate + NAD(P)+
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
the enzyme utilizes both NADH and NADPH as cofactors. The mode of cofactor binding to the enzyme is elucidated by determining the crystal structure of the enzyme in complex with NADP+
NADPH
the enzyme utilizes both NADH and NADPH as cofactors. The mode of cofactor binding to the enzyme is elucidated by determining the crystal structure of the enzyme in complex with NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
each protomer is composed of two domains, an N-terminal domain and a C-terminal domain. The N-terminal domain mainly contributes to nucleotide binding, whereas the C-terminal domain is involved in substrate binding
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme in the apoform and in complex with its cofactor NADP+, determined at 2.5 A resolution. The crystal belongs to the I4(1)22 space group, and the asymmetric unit of the crystal contains two CgDapB molecules
crystal structure of the enzyme in the apoform and in complex with its cofactor NADP+, hanging-drop vapor-diffusion method at 20°C, crystal structure of the enzyme is determined at 2.5 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subclone of gene dapB overexpressed in Corynebacterium glutamicum irrespective of orientation of the insert in the expression vector
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cremer, J.; Eggeling, L.; Sahm, H.
Cloning the dapA dapB cluster of the lysine-secreting bacterium Corynebacterium glutamicum
Mol. Gen. Genet.
220
478-480
1990
Corynebacterium glutamicum
-
Tosaka, O.; Takinami, K.
Pathway and regulation of lysine biosynthesis in Brevibacterium lactofermentum
Agric. Biol. Chem.
42
95-100
1978
Corynebacterium glutamicum
-
Sagong, H.Y.; Kim, K.J.
Structural insight into dihydrodipicolinate reductase from Corynebacterium glutamicum for lysine biosynthesis
J. Microbiol. Biotechnol.
26
226-232
2016
Corynebacterium glutamicum (P40110), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (P40110)
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