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Literature summary extracted from

  • Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H.
    A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. strain DK-38. Molecular cloning and cofactor characterization (1998), J. Biol. Chem., 273, 16678-16685.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.42 expression in Escherichia coli Arthrobacter sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.42 1.2
-
 DL-threo-beta-(3,4-dihydroxyphenylserine) pH 8.0, 30°C, with Mn2+ Arthrobacter sp.
4.1.2.42 1.4
-
 DL-threo-beta-(3,4-dihydroxyphenylserine) pH 8.0, 30°C, without Mn2+ Arthrobacter sp.
4.1.2.42 1.8
-
 DL-threo-beta-(3,4-methylenedioxyphenylserine) pH 8.0, 30°C, with Mn2+ Arthrobacter sp.
4.1.2.42 1.8
-
 DL-threo-beta-(3,4-methylenedioxyphenylserine) pH 8.0, 30°C, without Mn2+ Arthrobacter sp.
4.1.2.42 2
-
 DL-erythro-beta-(3,4-methylenedioxyphenylserine) pH 8.0, 30°C, without Mn2+ Arthrobacter sp.
4.1.2.42 2.5
-
 DL-erythro-beta-(3,4-methylenedioxyphenylserine) pH 8.0, 30°C, with Mn2+ Arthrobacter sp.
4.1.2.42 4.3
-
 D-allo-threonine pH 8.0, 30°C, without Mn2+ Arthrobacter sp.
4.1.2.42 4.4
-
 D-allo-threonine pH 8.0, 30°C, with Mn2+ Arthrobacter sp.
4.1.2.42 4.9
-
 DL-erythro-phenylserine pH 8.0, 30°C, without Mn2+ Arthrobacter sp.
4.1.2.42 5.3
-
 DL-erythro-phenylserine pH 8.0, 30°C, with Mn2+ Arthrobacter sp.
4.1.2.42 5.4
-
 DL-threo-phenylserine pH 8.0, 30°C, with Mn2+ Arthrobacter sp.
4.1.2.42 5.9
-
 DL-threo-phenylserine pH 8.0, 30°C, without Mn2+ Arthrobacter sp.
4.1.2.42 8.4
-
 D-threonine pH 8.0, 30°C, with Mn2+ Arthrobacter sp.
4.1.2.42 8.8
-
 D-threonine pH 8.0, 30°C, without Mn2+ Arthrobacter sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.42 Mn2+ activates, can bind 1 mol of Mn2+ per mol of subunit Arthrobacter sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.42 40000
-
 x * 40000, SDS-PAGE Arthrobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.42 Arthrobacter sp. O82872
-
-
4.1.2.42 Arthrobacter sp. DK-38 O82872
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.42 recombinant Arthrobacter sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.2.42 35.7
-
-
 Arthrobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.42 D-allo-threonine
-
 Arthrobacter sp. glycine + acetaldehyde
-
 r
4.1.2.42 D-allo-threonine
-
 Arthrobacter sp. DK-38 glycine + acetaldehyde
-
 r
4.1.2.42 D-threonine
-
 Arthrobacter sp. glycine + acetaldehyde
-
 r
4.1.2.42 D-threonine
-
 Arthrobacter sp. DK-38 glycine + acetaldehyde
-
 r
4.1.2.42 DL-erythro-beta-(3,4-methylenedioxyphenylserine)
-
 Arthrobacter sp. ?
-
 r
4.1.2.42 DL-erythro-beta-(3,4-methylenedioxyphenylserine)
-
 Arthrobacter sp. DK-38 ?
-
 r
4.1.2.42 DL-erythro-phenylserine
-
 Arthrobacter sp. glycine + benzaldehyde
-
 r
4.1.2.42 DL-erythro-phenylserine
-
 Arthrobacter sp. DK-38 glycine + benzaldehyde
-
 r
4.1.2.42 DL-threo-beta-(3,4-dihydroxyphenylserine)
-
 Arthrobacter sp. ?
-
 r
4.1.2.42 DL-threo-beta-(3,4-dihydroxyphenylserine)
-
 Arthrobacter sp. DK-38 ?
-
 r
4.1.2.42 DL-threo-beta-(3,4-methylenedioxyphenylserine)
-
 Arthrobacter sp. ?
-
 r
4.1.2.42 DL-threo-phenylserine
-
 Arthrobacter sp. glycine + benzaldehyde
-
 r
4.1.2.42 glycine + acetaldehyde
-
 Arthrobacter sp. D-threonine + D-allo-threonine
-
 r

Subunits

EC Number Subunits Comment Organism
4.1.2.42 ? x * 40000, SDS-PAGE Arthrobacter sp.

Synonyms

EC Number Synonyms Comment Organism
4.1.2.42 low specificity D-threonine aldolase
-
 Arthrobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.42 pyridoxal 5'-phosphate binds 1 mol of pyridoxal 5'-phosphate per mol of subunit, Lys59 is the cofactor binding site Arthrobacter sp.