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Literature summary for 4.1.2.13 extracted from

  • Krishnan, G.; Altekar, W.
    An unusual class I (Schiff base) fructose-1,6-bisphosphate aldolase from the halophilic archaebacterium Haloarcula vallismortis (1991), Eur. J. Biochem., 195, 343-350.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
arsenate causes further enhancement of enzyme activity when added iin 1-10 mM amounts in the standard assay medium containing KCl. Activity with 12 mM arsenate, is threefold higher than the original aldolase activity Haloarcula vallismortis
cysteine 1 mM, 1.3fold activation Haloarcula vallismortis
diphosphate causes further enhancement of enzyme activity when added in 1-10 mM amounts in the standard assay medium containing KCl Haloarcula vallismortis
phosphate causes further enhancement of enzyme activity when added in 1-10 mM amounts in the standard assay medium containing KCl Haloarcula vallismortis
reduced glutathione 1 mM, 1.4fold activation Haloarcula vallismortis

General Stability

General Stability Organism
the enzyme is totally inactivated within 75 min in 0.5 - 0.05 mM Tris/HCI pH 8.0, whereas 80% activity is retained in 3 M KCl, 50 mM Tris/HCI pH 8.0 at the end of 72 h. Addition of 1 M (NH4)2S04 to the enzyme in 1.5 M KCI stabilizes the enzyme activity for at least 48 h Haloarcula vallismortis

Inhibitors

Inhibitors Comment Organism Structure
(NH4)2SO4
-
Haloarcula vallismortis
5,5'-dithiobis(2-nitrobenzoic acid) 1 mM, complete inhibition Haloarcula vallismortis
CuCl2 1 mM, complete inhibition Haloarcula vallismortis
EDTA 1 mM, 7% inhibition Haloarcula vallismortis
HgCl2 1 mM, complete inhibition Haloarcula vallismortis
iodoacetate 1 mM, 46% inhibition Haloarcula vallismortis
NaNO3
-
Haloarcula vallismortis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.38
-
D-fructose 1,6-bisphosphate pH 7.5, 37°C Haloarcula vallismortis
28
-
D-Fructose 1-phosphate pH 7.5, 37°C Haloarcula vallismortis

Metals/Ions

Metals/Ions Comment Organism Structure
KCl the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI Haloarcula vallismortis
LiCl the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI Haloarcula vallismortis
NaCl the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI Haloarcula vallismortis
NH4Cl the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI Haloarcula vallismortis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
10 * 27000 Haloarcula vallismortis
280000
-
gel filtration Haloarcula vallismortis

Organism

Organism UniProt Comment Textmining
Haloarcula vallismortis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Haloarcula vallismortis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
38.4
-
pH 7.5, 37°C Haloarcula vallismortis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate
-
Haloarcula vallismortis glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?
D-Fructose 1-phosphate the D-fructose 1,6-bisphosphate/D-fructose 1-phosphate cleavage ratio is 55:1 Haloarcula vallismortis Glycerone phosphate + D-glyceraldehyde
-
?

Subunits

Subunits Comment Organism
decamer 10 * 27000 Haloarcula vallismortis

Synonyms

Synonyms Comment Organism
fructose-1,6-bisphosphate aldolase
-
Haloarcula vallismortis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Haloarcula vallismortis
41
-
-
Haloarcula vallismortis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
56
-
aldolase activity, which is lost within 2 min at 56°C, can be retained for 30 min at the same temperature in the presence of 100 mM phosphate Haloarcula vallismortis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Haloarcula vallismortis