Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Marini, I.; Moschini, R.; Del Corso, A.; Mura, U.
    Complete protection by alpha-crystallin of lens sorbitol dehydrogenase undergoing thermal stress (2000), J. Biol. Chem., 275, 32559-32565.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.1.1.14 alpha-crystallin stabilizes Bos taurus
1.1.1.14 bovine serum albumin stabilizes Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.14 Bos taurus
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.14 D-fructose + NADH + H+
-
Bos taurus D-sorbitol + NAD+
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.14 18
-
50% loss of activity after 40 min, alpha-crystallin protects fully against activity loss Bos taurus
1.1.1.14 45
-
50% loss of activity after 20 min, alpha-crystallin protects fully against activity loss Bos taurus
1.1.1.14 55
-
50% loss of activity after 10 min, alpha-crystallin protects fully against activity loss Bos taurus
1.1.1.14 60
-
50% loss of activity after 5 min, alpha-crystallin reduces activity loss by 50% Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.14 NAD+
-
Bos taurus
1.1.1.14 NADH
-
Bos taurus