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Literature summary for 5.1.3.3 extracted from

  • Fishman, P.H.; Kusiak, J.W.; Bailey, J.M.
    Studies on mutarotase: photooxidation reactions and nature of the enzyme catalysis (1973), Biochemistry, 12, 2540-2544.
    View publication on PubMed
Search for more literature for 5.1.3.3

General Stability

General Stability Organism
photoinactivation in presence of methylene blue or rose bengal. A constant photoinactivation rate is observed in the range pH 5.5-8.0 which increases rapidly at higher values. The competitive inhibitor Hg2+ increases the photosensitivity of the enzyme. The competitive inhibitors, L-fucose and L-xylose protect from photoinactivation Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
alpha-methyl-D-glucoside competitive Bos taurus
Hg2+ competitive Bos taurus
L-fucose competitive Bos taurus
L-Xylose competitive Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
alpha-D-glucose = beta-D-glucose Trp is involved as glucose-binding site and catalysis of the mutarotation reaction is accomplished by a ring-distortion type of mechanism Bos taurus
a

Source Tissue

Source Tissue Comment Organism Textmining
kidney cortex Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-glucose
-
 Bos taurus beta-D-glucose
-
 ?