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Literature summary extracted from

  • Dogovski, C.; Dommaraju, S.R.; Small, L.C.; Perugini, M.A.
    Comparative structure and function analyses of native and his-tagged forms of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus (2012), Protein Expr. Purif., 85, 66-76.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.1.8 expressed in Escherichia coli BL21(DE3) cells Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.1.8 0.006
-
NADH recombinant enzyme, at pH 8.0 and 30°C Staphylococcus aureus
1.17.1.8 0.022
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate recombinant enzyme, at pH 8.0 and 30°C Staphylococcus aureus
1.17.1.8 0.026
-
NADH native enzyme, at pH 8.0 and 30°C Staphylococcus aureus
1.17.1.8 0.039
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate native enzyme, at pH 8.0 and 30°C Staphylococcus aureus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.17.1.8 27622
-
4 * 27622, calculated from amino acid sequence Staphylococcus aureus
1.17.1.8 27622
-
4 * 27622, ESI-TOF mass spectrometry Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.8 Staphylococcus aureus
-
-
-
1.17.1.8 Staphylococcus aureus MRSA
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.8 Ni2+ affinity column chromatography and Superose 12 gel filtration Staphylococcus aureus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.17.1.8 additional information
-
at pH 8.0 and 30°C, the crude recombinant enzyme and enzyme after 2.9fold purification show specific activities of 5.51 and 16 units/mg, respectively Staphylococcus aureus

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 + NADH + H+
-
Staphylococcus aureus (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
-
ir
1.17.1.8 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
-
Staphylococcus aureus MRSA (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O
-
ir
1.17.1.8 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
Staphylococcus aureus (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
-
ir
1.17.1.8 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+
-
Staphylococcus aureus MRSA (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O
-
ir

Subunits

EC Number Subunits Comment Organism
1.17.1.8 homotetramer 4 * 27622, calculated from amino acid sequence Staphylococcus aureus
1.17.1.8 homotetramer 4 * 27622, ESI-TOF mass spectrometry Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
1.17.1.8 DapB
-
Staphylococcus aureus
1.17.1.8 DHDPR
-
Staphylococcus aureus
1.17.1.8 dihydrodipicolinate reductase
-
Staphylococcus aureus
1.17.1.8 EC 1.3.1.26 formerly Staphylococcus aureus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.17.1.8 65
-
both the native and His-tagged recombinant enzymes show an apparent melting temperature of approximately 65°C Staphylococcus aureus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.17.1.8 20
-
NADH native enzyme, at pH 8.0 and 30°C Staphylococcus aureus
1.17.1.8 20
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate native enzyme, at pH 8.0 and 30°C Staphylococcus aureus
1.17.1.8 21
-
NADH recombinant enzyme, at pH 8.0 and 30°C Staphylococcus aureus
1.17.1.8 21
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate recombinant enzyme, at pH 8.0 and 30°C Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.8 NADH
-
Staphylococcus aureus
1.17.1.8 NADPH
-
Staphylococcus aureus

General Information

EC Number General Information Comment Organism
1.17.1.8 metabolism the enzyme catalyzes the second step of the lysine biosynthesis pathway Staphylococcus aureus