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Literature summary for 1.14.11.39 extracted from

  • Strieker, M.; Kopp, F.; Mahlert, C.; Essen, L.O.; Marahiel, M.A.
    Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide (2007), ACS Chem. Biol., 2, 187-196.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as His7-tagged fusion Streptomyces coelicolor

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are grown at 18°C by the sitting-drop vapordiffusion method, 1.45 A, 1.92 A and 1.66 A crystal structures of AsnO as apoprotein, Fe2+ complex, and product complex, respectively, with (2S,3S)-3-hydroxyasparagine and succinate Streptomyces coelicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.479
-
L-asparagine pH 7.5, 25°C Streptomyces coelicolor

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ non-heme Fe2+ enzyme Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-asparagine + 2-oxoglutarate + O2 Streptomyces coelicolor the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone (2S,3S)-3-hydroxyasparagine + succinate + CO2
-
?
L-asparagine + 2-oxoglutarate + O2 Streptomyces coelicolor A3(2) the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone (2S,3S)-3-hydroxyasparagine + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor Q9Z4Z5
-
-
Streptomyces coelicolor A3(2) Q9Z4Z5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-asparagine + 2-oxoglutarate + O2 the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone Streptomyces coelicolor (2S,3S)-3-hydroxyasparagine + succinate + CO2
-
?
L-asparagine + 2-oxoglutarate + O2 the enzyme exclusively acts on free L-asparagine. It is not active toward D-asparagine Streptomyces coelicolor (2S,3S)-3-hydroxyasparagine + succinate + CO2
-
?
L-asparagine + 2-oxoglutarate + O2 the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone Streptomyces coelicolor A3(2) (2S,3S)-3-hydroxyasparagine + succinate + CO2
-
?
L-asparagine + 2-oxoglutarate + O2 the enzyme exclusively acts on free L-asparagine. It is not active toward D-asparagine Streptomyces coelicolor A3(2) (2S,3S)-3-hydroxyasparagine + succinate + CO2
-
?

Synonyms

Synonyms Comment Organism
AsnO
-
Streptomyces coelicolor
L-asparagine 3-hydroxylase
-
Streptomyces coelicolor

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.98
-
L-asparagine pH 7.5, 25°C Streptomyces coelicolor

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
10.4
-
L-asparagine pH 7.5, 25°C Streptomyces coelicolor