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Literature summary for 4.1.2.42 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)

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Arthrobacter sp. O82872
-
-
Arthrobacter sp. DK-38 O82872
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Arthrobacter sp.

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Cofactor

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