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Literature summary for 4.1.1.9 extracted from

  • Robbel, L.; Helmetag, V.; Knappe, T.A.; Marahiel, M.A.
    Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin (2011), Biochemistry, 50, 6073-6080.
    View publication on PubMed
Search for more literature for 4.1.1.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Saccharopolyspora erythraea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025
-
 N-hydroxy-L-ornithine in 20 mM Tris, 100 mM NaCl, pH 7.2, at 25°C Saccharopolyspora erythraea

Organism

Organism UniProt Comment Textmining
Saccharopolyspora erythraea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Saccharopolyspora erythraea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Malonyl-CoA
-
 Saccharopolyspora erythraea Acetyl-CoA + CO2
-
 ?
N-hydroxy-L-ornithine + malonyl-CoA acetylation of the delta-amino functionality of N-hydroxy-L-ornithine is mediated by the bifunctional malonyl-CoA decarboxylase/acetyltransferase Mcd Saccharopolyspora erythraea delta-N-acetyl-delta-N-hydroxy-L-ornithine + coenzyme A + CO2
-
 ?

Synonyms

Synonyms Comment Organism
malonyl-CoA decarboxylase/acetyltransferase bifunctional enzyme Saccharopolyspora erythraea
MCD bifunctional enzyme Saccharopolyspora erythraea

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.038
-
 N-hydroxy-L-ornithine in 20 mM Tris, 100 mM NaCl, pH 7.2, at 25°C Saccharopolyspora erythraea

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.53
-
 N-hydroxy-L-ornithine in 20 mM Tris, 100 mM NaCl, pH 7.2, at 25°C Saccharopolyspora erythraea