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Information on EC 1.17.1.8 - 4-hydroxy-tetrahydrodipicolinate reductase and Organism(s) Pseudomonas aeruginosa

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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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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
Synonyms
dihydrodipicolinate reductase, dhdpr, mrsa-dhdpr, dihydrodipicolinic acid reductase, 4-hydroxy-tetrahydrodipicolinate reductase, abdhdpr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrodipicolinate reductase
-
-
dihydrodipicolinic acid reductase
-
-
-
-
EC 1.3.1.26
-
formerly
reductase, dihydrodipicolinate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
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
-
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 + NADH + H+
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
show the reaction diagram
-
-
-
-
ir
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
show the reaction diagram
-
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.05
NADPH
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
at pH 7.0 and 9.0, approyimately 75% and 90% of the enzymatic activity is retained. Below pH 7.0 and above pH 9.0 a significant drop in activity is observed. At pH 11.0 an almost complete loss of activity is observed
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
at 30°C and 50°C, approximately 57% and 85% of the enzymatic activity is retained. Between 50 and 60°C a fast decrease in activity is observed with increasing temperature. Complete loss of activity occurs above 60°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G4M613_PSEAI
268
0
28225
TrEMBL
-
A0A8G4TLX2_PSEAI
268
0
28294
TrEMBL
-
A0A8G2TX78_PSEAI
268
0
28294
TrEMBL
-
A0A0A8RHI3_PSEAI
268
0
28350
TrEMBL
-
A0A8G2Z180_PSEAI
268
0
28343
TrEMBL
-
A0A3M5ERA0_PSEAI
282
0
30254
TrEMBL
-
A0A8G7NJT7_PSEAI
268
0
28323
TrEMBL
-
A0A8G7AQ57_PSEAI
268
0
28354
TrEMBL
-
A0A8G7L355_PSEAI
268
0
28310
TrEMBL
-
A0A072ZKT6_PSEAI
268
0
28324
TrEMBL
-
A0A2R3J357_PSEAI
268
0
28325
TrEMBL
-
A0A8G6CVH3_PSEAI
268
0
28352
TrEMBL
-
A0A3S3U242_PSEAI
268
0
28324
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
gel filtration
28000
-
4 * 28000, calculated from amino acid sequence
30000
-
4 * 30000, His-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anand, V.; Gautam, A.; Sareen, D.; Singh, T.; Tewari, R.
Molecular cloning, biochemical and biophysical studies of dihydrodipicolinate reductase of Pseudomonas aeruginosa PAO1
Int. J. Integr. Biol.
11
145-152
2011
Pseudomonas aeruginosa
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Manually annotated by BRENDA team