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Literature summary for 1.1.1.27 extracted from

  • Madern, D.; Cai, X.; Abrahamsen, M.S.; Zhu, G.
    Evolution of Cryptosporidium parvum lactate dehydrogenase from malate dehydrogenase by a very recent event of gene duplication (2003), Mol. Biol. Evol., 21, 489-497.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli as maltose-binding protein fusion protein. CpLDH1 is probably evolved from the same ancestor of CpMalDH1 by a very recent gene duplication that occurs after Cryptosporidium parvum diverges from other apocomplexans Cryptosporidium parvum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
pyruvate pH 8.0, 25°C Cryptosporidium parvum
0.5
-
NADH pH 8.0, 25°C Cryptosporidium parvum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
77000
-
monomer, sedimentation velocity Cryptosporidium parvum
134000
-
dimer, sedimentation velocity Cryptosporidium parvum

Organism

Organism UniProt Comment Textmining
Cryptosporidium parvum Q9GT92
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + NADH + H+
-
Cryptosporidium parvum (S)-lactate + NAD+
-
?

Subunits

Subunits Comment Organism
dimer 2 * 77000, monomer-dimer equilibrium in solution Cryptosporidium parvum
monomer 1 * 77000, monomer-dimer equilibrium in solution Cryptosporidium parvum

Synonyms

Synonyms Comment Organism
LDH
-
Cryptosporidium parvum

Cofactor

Cofactor Comment Organism Structure
NADH
-
Cryptosporidium parvum