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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.1.8 (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
1.17.1.8 (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
1.17.1.8 (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
1.17.1.8 (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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.1.8 0.0005
-
NADH pH 8.0, 25°C Neisseria meningitidis
1.17.1.8 0.0014
-
NADH pH 8.0, 25°C Selaginella moellendorffii
1.17.1.8 0.0031
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Vitis vinifera
1.17.1.8 0.0047
-
NADH pH 8.0, 25°C Vitis vinifera
1.17.1.8 0.0068
-
NADPH pH 8.0, 25°C Selaginella moellendorffii
1.17.1.8 0.0092
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Vitis vinifera
1.17.1.8 0.012
-
NADPH pH 8.0, 25°C Neisseria meningitidis
1.17.1.8 0.012
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Selaginella moellendorffii
1.17.1.8 0.013
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Neisseria meningitidis
1.17.1.8 0.016
-
NADPH pH 8.0, 25°C Vitis vinifera
1.17.1.8 0.058
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Selaginella moellendorffii
1.17.1.8 0.085
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Neisseria meningitidis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.17.1.8 62900
-
calculated Vitis vinifera
1.17.1.8 64200
-
calculated Selaginella moellendorffii
1.17.1.8 113000
-
calculated Neisseria meningitidis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.1.8 (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
-
?
1.17.1.8 (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
-
?
1.17.1.8 (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
-
?
1.17.1.8 (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

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.8 (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
-
?
1.17.1.8 (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
-
?
1.17.1.8 (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
-
?
1.17.1.8 (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
-
?
1.17.1.8 (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
-
?
1.17.1.8 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
Selaginella moellendorffii (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
-
?
1.17.1.8 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
Vitis vinifera (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
-
?
1.17.1.8 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
Neisseria meningitidis (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
-
?
1.17.1.8 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
Selaginella moellendorffii (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
-
?
1.17.1.8 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
Vitis vinifera (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
-
?
1.17.1.8 (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

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.1.8 25
-
assay at Selaginella moellendorffii
1.17.1.8 25
-
assay at Arabidopsis thaliana
1.17.1.8 25
-
assay at Vitis vinifera
1.17.1.8 25
-
assay at Neisseria meningitidis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.17.1.8 14
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Vitis vinifera
1.17.1.8 21
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Vitis vinifera
1.17.1.8 43
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Neisseria meningitidis
1.17.1.8 49
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Selaginella moellendorffii
1.17.1.8 63
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Selaginella moellendorffii
1.17.1.8 77
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Neisseria meningitidis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.1.8 8
-
assay at Selaginella moellendorffii
1.17.1.8 8
-
assay at Arabidopsis thaliana
1.17.1.8 8
-
assay at Vitis vinifera
1.17.1.8 8
-
assay at Neisseria meningitidis

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.8 NADH
-
Selaginella moellendorffii
1.17.1.8 NADH
-
Vitis vinifera
1.17.1.8 NADPH
-
Selaginella moellendorffii
1.17.1.8 NADPH
-
Vitis vinifera

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.17.1.8 0.032
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Selaginella moellendorffii
1.17.1.8 0.76
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Vitis vinifera
1.17.1.8 1.3
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Selaginella moellendorffii
1.17.1.8 1.8
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADPH Vitis vinifera
1.17.1.8 5.5
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate pH 8.0, 25°C, cofactor: NADH Neisseria meningitidis

General Information

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