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Literature summary for 1.1.1.21 extracted from

  • Moschini, R.; Marini, I.; Malerba, M.; Cappiello, M.; Del Corso, A.; Mura, U.
    Chaperone-like activity of alpha-crystallin toward aldose reductase oxidatively stressed by copper ion (2006), Arch. Biochem. Biophys., 453, 13-17.
    View publication on PubMed

General Stability

General Stability Organism
alpha-crystallin stabilizes the enzyme with higher efficiency at 37°C compared to 25°C Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ oxidative inactivation of ALR2, ratio Cu2+ to enzyme of 2:1, precipitation of the enzyme occurs at higher Cu2+ concentration, alpha-crystallin stabilizes the enzyme and protects against inactivation and precipitation by Cu2+ with higher efficiency at 37°C compared to 25°C, overview Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
lens
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DL-glyceraldehyde + NADPH + H+
-
Bos taurus glycerol + NADP+
-
?

Synonyms

Synonyms Comment Organism
aldose reductase
-
Bos taurus
ALR2
-
Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Bos taurus