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Literature summary for 1.17.1.8 extracted from

  • Sagong, H.Y.; Kim, K.J.
    Structural insight into dihydrodipicolinate reductase from Corynebacterium glutamicum for lysine biosynthesis (2016), J. Microbiol. Biotechnol., 26, 226-232 .
    View publication on PubMed
Search for more literature for 1.17.1.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in an Escherichia coli B834 strain Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Corynebacterium glutamicum
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 Corynebacterium glutamicum

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+ Corynebacterium glutamicum 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+ Corynebacterium glutamicum ATCC 13032 the enzyme is involved in L-lysine biosynthesis (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
-
 ?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O Corynebacterium glutamicum 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 Corynebacterium glutamicum ATCC 13032 involved in L-lysine biosynthesis (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum P40110
-
-
Corynebacterium glutamicum ATCC 13032 P40110
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Corynebacterium glutamicum

Reaction

Reaction Comment Organism Reaction ID
(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 Corynebacterium glutamicum
a

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+ the enzyme is involved in L-lysine biosynthesis Corynebacterium glutamicum (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+ it is proposed that the the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme Corynebacterium glutamicum (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 is involved in L-lysine biosynthesis Corynebacterium glutamicum ATCC 13032 (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+ it is proposed that the the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme Corynebacterium glutamicum ATCC 13032 (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O
-
 ?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O involved in L-lysine biosynthesis Corynebacterium glutamicum (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 involved in L-lysine biosynthesis Corynebacterium glutamicum ATCC 13032 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
-
 ?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
 ?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum ATCC 13032 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
 ?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
 ?
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum ATCC 13032 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 260240, calculated from sequence Corynebacterium glutamicum
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 Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
DapB
-
 Corynebacterium glutamicum
dihydrodipicolinate reductase
-
 Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
NADH the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum
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+ Corynebacterium glutamicum
NADPH the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum
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+ Corynebacterium glutamicum

General Information

General Information Comment Organism
metabolism the enzyme is involved in L-lysine biosynthesis Corynebacterium glutamicum