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Literature summary for 1.1.1.14 extracted from

  • Marini, I.; Moschini, R.; Del Corso, A.; Mura, U.
    alpha-Crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase (2005), Cell. Mol. Life Sci., 62, 599-605.
    View publication on PubMed

General Stability

General Stability Organism
complete renaturation, alpha-crystallin has the ability to elicit protein refolding. This action of alpha-crystallin appears not to be dependent on ATP as energy donor, but essentially associated with intrinsic structural features of this chaperone molecule Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
-
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.
D-fructose + NADH + H+
-
Bos taurus D-sorbitol + NAD+
-
?

Synonyms

Synonyms Comment Organism
SDH
-
Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADH
-
Bos taurus