Literature summary 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.

Inhibitors

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

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.1.1.21	34000	-	isozyme ALR 2, gel filtration	Bos taurus

Organism

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

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.1.1.21	ALR 2	Bos taurus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.1.1.21	lens	-	Bos taurus	-

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.1.1.21	1.2	-	NADPH, purified enzyme	Bos taurus

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
1.1.1.21	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

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Release 2023.1 (January 2023)