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Literature summary for 4.1.2.13 extracted from

  • D'Souza, S.E.; Altekar, W.
    A class II fructose-1,6-bisphosphate aldolase from a halophilic archaebacterium Haloferax mediterranei (1998), J. Gen. Appl. Microbiol., 44, 235-241.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol up to 5 mM, enhances enzyme activity twofold Haloferax mediterranei

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 2 mM, 85% inhibition Haloferax mediterranei
2,2'-bipyridyl 2 mM, 76% inhibition Haloferax mediterranei
EDTA 2 mM, complete inhibition. Activity can be completely restored only by Fe2+. Other divalent metal ions such as Mn2+, Mg2+, and Zn2+ have no effect. Co2+ and Ca2+ can restore 20% and 10%, respectively, of enzyme activity Haloferax mediterranei
Fe2+ optimum aldolase activity (137%) is observed with 1.0 mM Fe2+ concentration. Inhibition at concentrations baove 1.0 mM Haloferax mediterranei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2
-
D-fructose 1,6-bisphosphate pH 7.5, 37°C Haloferax mediterranei

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ can restore 10% of enzyme activity after complete inhibition by EDTA treatment (2 mM) Haloferax mediterranei
Co2+ can restore 20% of enzyme activity after complete inhibition by EDTA treatment (2 mM) Haloferax mediterranei
Fe2+ optimum aldolase activity (137%) is observed with 1.0 mM Fe2+ concentration. Inhibition at concentrations above 1.0 mM. Activity of the enzyme completely inhibited by EDTA (2 mM) can be completely restored by Fe2+ Haloferax mediterranei
KCl aldolase activity increases with an increasing concentration of KCl. At 4.0 M KCl concentration, activity is 2.5 times that at 0.5 M KCl concentration. Enzyme activity is appreciable even in the absence of added salt Haloferax mediterranei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
2 * 50000, SDS-PAGE Haloferax mediterranei
110000
-
sucrose density gradient ultracentrifugation Haloferax mediterranei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-fructose 1,6-bisphosphate Haloferax mediterranei
-
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?
D-fructose 1,6-bisphosphate Haloferax mediterranei DSM 1411
-
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Haloferax mediterranei
-
-
-
Haloferax mediterranei DSM 1411
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Haloferax mediterranei

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.8
-
pH 7.5, 37°C Haloferax mediterranei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate
-
Haloferax mediterranei glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?
D-fructose 1,6-bisphosphate
-
Haloferax mediterranei DSM 1411 glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 50000, SDS-PAGE Haloferax mediterranei

Synonyms

Synonyms Comment Organism
class II fructose-1,6-bisphosphate aldolase
-
Haloferax mediterranei
FBP aldolase
-
Haloferax mediterranei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Haloferax mediterranei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8 broad pH optimum in glycylglycine buffer and imidazole buffer Haloferax mediterranei
7.5
-
in Tris-HCl buffer Haloferax mediterranei