Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.3.41 extracted from

  • Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.
    A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning (2003), Appl. Microbiol. Biotechnol., 62, 53-60.
    View publication on PubMed
Search for more literature for 4.1.3.41

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli XL1-Blue MRF‘ cells Paracoccus denitrificans

Inhibitors

Inhibitors Comment Organism Structure
EDTA 82% inhibition at 1 mM Paracoccus denitrificans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
 D-erythro-3-hydroxyaspartate in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 2.0fold increase of specific activity in the presence of 1 mM Co2+ Paracoccus denitrificans
Mg2+ 5.4fold increase of specific activity in the presence of 1 mM Mg2+ Paracoccus denitrificans
Mn2+ 8.1fold increase of specific activity in the presence of 1 mM Mn2+ Paracoccus denitrificans
additional information K+ and Na+ do not have an effect on the enzymatic activity Paracoccus denitrificans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41633
-
 2 * 41633, calculated from amino acid sequence Paracoccus denitrificans
43000
-
 2 * 43000, SDS-PAGE Paracoccus denitrificans
80000
-
 gel filtration Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans Q8GRC8 strain IFO 13301
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate fractionation, hydroxyapatite column chromatography, DEAE-Toyopearl column chromatography, phenyl-Toyopearl column chromatography, Superdex 200 gel filtration, and Mono Q column chromatography Paracoccus denitrificans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.36
-
 after 50fold purification, using DL-threo-3-hydroxyaspartate as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans
0.6
-
 crude extract, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans
14.6
-
 after 50fold purification, using D-threo-3-3,4-methylenedioxyphenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans
17.5
-
 after 50fold purification, using D-erythro-3-3,4-methylenedioxyphenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans
20
-
 after 50fold purification, using D-threonine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans
25
-
 after 50fold purification, using D-allo-threonine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans
30
-
 after 50fold purification, using D-erythro-3-hydroxyaspartate as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans
95
-
 after 50fold purification, using D-threo-3-phenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans
99
-
 after 50fold purification, using D-erythro-3-phenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C Paracoccus denitrificans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-amino-3-hydroxybutanedioic acid
-
 Paracoccus denitrificans aminoacetic acid + oxoacetic acid
-
 r
allo-threonine
-
 Paracoccus denitrificans ?
-
 ?
D-3-3,4-dihydroxyphenylserine
-
 Paracoccus denitrificans ?
-
 ?
D-erythro-3-3,4-methylenedioxyphenylserine
-
 Paracoccus denitrificans ?
-
 ?
D-erythro-3-hydroxyaspartate the enzyme is strictly D-specific as to the alpha-position, whereas it does not distinguish between threo and erythro forms at the beta-position Paracoccus denitrificans glycine + glyoxylate
-
 ?
D-erythro-3-phenylserine
-
 Paracoccus denitrificans ?
-
 ?
D-threo-3-3,4-methylenedioxyphenylserine
-
 Paracoccus denitrificans ?
-
 ?
D-threo-3-phenylserine
-
 Paracoccus denitrificans ?
-
 ?
additional information the enzyme shows no activity towards L-erythro-3-hydroxyaspartate, L-threo-3-hydroxyaspartate, L-threonine, L-allo-threonine, L-erythro-3-phenylserine, L-threo-3-phenylserine, L-erythro-3-3,4-methylenedioxyphenylserine, and L-threo-3-3,4-methylenedioxyphenylserine Paracoccus denitrificans ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 43000, SDS-PAGE Paracoccus denitrificans
homodimer 2 * 41633, calculated from amino acid sequence Paracoccus denitrificans

Synonyms

Synonyms Comment Organism
D-3-hydroxyaspartate aldolase
-
 Paracoccus denitrificans
d-HAA
-
 Paracoccus denitrificans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Paracoccus denitrificans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 the enzyme retains 50% activity upon heating at 45°C for 30 min Paracoccus denitrificans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Paracoccus denitrificans

pH Range

pH Minimum pH Maximum Comment Organism
7.5 10
-
 Paracoccus denitrificans

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.5 8.5 the enzyme is stable between pH 6.5 and 8.5 for 30 min at 30°C Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Paracoccus denitrificans