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Literature summary for 1.1.1.21 extracted from

  • Marini, I.; Bucchioni, L.; Voltarelli, M.; Del Corso, A.; Mura, U.
    Alpha-crystallin-like molecular chaperone against the thermal denaturation of lens aldose reductase: the effect of divalent metal ions (1995), Biochem. Biophys. Res. Commun., 212, 413-420.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 10 mM inhibits complex formation of ALR 2 with alpha-crystallin Bos taurus
Mg2+ 10 mM inhibits complex formation of ALR 2 with alpha-crystallin, induces ALR 2 aggregation and precipitation Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
isozyme ALR 2, gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
2 enzymes AR I (ALR 1) and AR II (ALR 2)
-

Purification (Commentary)

Purification (Comment) Organism
ALR 2 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
lens
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2
-
NADPH, purified enzyme Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DL-glyceraldehyde + NAD(P)H
-
Bos taurus glycerol + NAD(P)+
-
r

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
thermal aggregation and precipitation is prevented by specific, thermal stress induced complexing of alpha-crystallin, stable at least for 2 h at 55°C and for hours at room temperature, complexing can be hindered by Tris Bos taurus