Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.17.1.8 extracted from

  • 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 (2018), Biochem. J., 475, 137-150 .
    View publication on PubMed
Search for more literature for 1.17.1.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) cells Vitis vinifera

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapour-diffusion method Selaginella moellendorffii
sitting-drop vapour-diffusion method Neisseria meningitidis
vapour-diffusion method Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
(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 Arabidopsis thaliana
(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 Neisseria meningitidis
(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 Selaginella moellendorffii
(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 Vitis vinifera

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0005
-
 NADH pH 8.0, 25°C Neisseria meningitidis
0.0014
-
 NADH pH 8.0, 25°C Selaginella moellendorffii
0.0031
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Vitis vinifera
0.0047
-
 NADH pH 8.0, 25°C Vitis vinifera
0.0068
-
 NADPH pH 8.0, 25°C Selaginella moellendorffii
0.0092
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Vitis vinifera
0.012
-
 NADPH pH 8.0, 25°C Neisseria meningitidis
0.012
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Selaginella moellendorffii
0.013
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Neisseria meningitidis
0.016
-
 NADPH pH 8.0, 25°C Vitis vinifera
0.058
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Selaginella moellendorffii
0.085
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Neisseria meningitidis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62900
-
 calculated Vitis vinifera
64200
-
 calculated Selaginella moellendorffii
113000
-
 calculated Neisseria meningitidis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ Neisseria meningitidis
-
 (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+ Selaginella moellendorffii the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants (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+ Arabidopsis thaliana the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants (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+ Vitis vinifera the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8LB01
-
-
Neisseria meningitidis Q9K1F1
-
-
Selaginella moellendorffii D8R6G2
-
-
Vitis vinifera F6HB41
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
-
 Arabidopsis thaliana (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+
-
 Neisseria meningitidis (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 enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants Selaginella moellendorffii (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 enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants Arabidopsis thaliana (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 enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants Vitis vinifera (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
-
 ?
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
 Selaginella moellendorffii (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
-
 ?
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
 Vitis vinifera (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
-
 ?
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
 Neisseria meningitidis (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
-
 ?
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
 Selaginella moellendorffii (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
-
 ?
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
 Vitis vinifera (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
-
 ?
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
 Neisseria meningitidis (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
-
 ?

Subunits

Subunits Comment Organism
dimer the dimer forms through the intra-strand interface. Unique secondary features in plant enzymes block tetramer assembly Selaginella moellendorffii
dimer the dimer forms through the intra-strand interface. Unique secondary features in plant enzymes block tetramer assembly Arabidopsis thaliana
dimer the dimer forms through the intra-strand interface. Unique secondary features in plant enzymes block tetramer assembly Vitis vinifera
tetramer
-
 Neisseria meningitidis

Synonyms

Synonyms Comment Organism
DapB
-
 Neisseria meningitidis
DHDPR
-
 Selaginella moellendorffii
DHDPR
-
 Arabidopsis thaliana
DHDPR
-
 Vitis vinifera
DHDPR
-
 Neisseria meningitidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Selaginella moellendorffii
25
-
 assay at Arabidopsis thaliana
25
-
 assay at Vitis vinifera
25
-
 assay at Neisseria meningitidis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
14
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Vitis vinifera
21
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Vitis vinifera
43
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Neisseria meningitidis
49
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Selaginella moellendorffii
63
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Selaginella moellendorffii
77
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Neisseria meningitidis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Selaginella moellendorffii
8
-
 assay at Arabidopsis thaliana
8
-
 assay at Vitis vinifera
8
-
 assay at Neisseria meningitidis

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Selaginella moellendorffii
NADH
-
 Vitis vinifera
NADPH
-
 Selaginella moellendorffii
NADPH
-
 Vitis vinifera

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.032
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Selaginella moellendorffii
0.76
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Vitis vinifera
1.3
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Selaginella moellendorffii
1.8
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Vitis vinifera
5.5
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Neisseria meningitidis

General Information

General Information Comment Organism
metabolism the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants Selaginella moellendorffii
metabolism the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants Arabidopsis thaliana
metabolism the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants Vitis vinifera