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Literature summary extracted from

  • Farkas, W.; Gilvarg, C.
    The reduction step in diaminopimelic acid biosynthesis (1965), J. Biol. Chem., 240, 4717-4722.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.1.8 2,3-dihydrodipicolinate + NAD(P)H Escherichia coli determination of metabolic block in the pathway in mutant M-203 2,3,4,5-tetrahydrodipicolinate + NAD(P)+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.8 Escherichia coli
-
 mutant M-203 with with a requirement for lysine and diaminopimelate
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.8 purified from wild-type Escherichia coli

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 15.4
-
-
 Escherichia coli

Storage Stability

EC Number Storage Stability Organism
1.17.1.8 -15°C, several months Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.8 2,3-dihydrodipicolinate + NAD(P)H
-
 Escherichia coli 2,3,4,5-tetrahydrodipicolinate + NAD(P)+
-
 ?
1.17.1.8 2,3-dihydrodipicolinate + NAD(P)H determination of metabolic block in the pathway in mutant M-203 Escherichia coli 2,3,4,5-tetrahydrodipicolinate + NAD(P)+
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.17.1.8 70
-
 3 min stable Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.8 NADH 47% of activity compared to that with NADPH Escherichia coli
1.17.1.8 NADPH
-
 Escherichia coli