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Information on EC 1.17.1.8 - 4-hydroxy-tetrahydrodipicolinate reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8LB01

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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Arabidopsis thaliana
UNIPROT: Q8LB01
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
dihydrodipicolinate reductase-like protein
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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
(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
show the reaction diagram
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
(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
show the reaction diagram
the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate
dihydrodipicolinate reductase enzymes from plants are much more prone to substrate inhibition than the bacterial enzymes, which appears to be a consequence of increased flexibility of the substrate-binding loop and higher affinity for the nucleotide substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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specifically expressed in leaves
Manually annotated by BRENDA team
additional information
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not found in roots
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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not in the thylakoid membranes
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DAPB2_ARATH
349
0
37870
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29200
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predicted molecular weight of mature CRR1
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the dimer forms through the intra-strand interface. Unique secondary features in plant enzymes block tetramer assembly
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour-diffusion method
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimizu, H.; Shikanai, T.
Dihydrodipicolinate reductase-like protein, CRR1, is essential for chloroplast NAD(P)H dehydrogenase in Arabidopsis
Plant J.
52
539-547
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Watkin, S.A.J.; Keown, J.R.; Richards, E.; Goldstone, D.C.; Devenish, S.R.A.; Grant Pearce, F.
Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly
Biochem. J.
475
137-150
2018
Arabidopsis thaliana (Q8LB01), Neisseria meningitidis (Q9K1F1), Selaginella moellendorffii (D8R6G2), Vitis vinifera (F6HB41)
Manually annotated by BRENDA team