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Literature summary for 5.1.3.3 extracted from

  • Toyoda, Y.; Miwa, I.; Okuda, J.
    Purification and characterization of multiple forms of mutarotase from hog kidney cortex (1982), J. Biochem., 91, 1889-1898.
    View publication on PubMed
Search for more literature for 5.1.3.3

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
19
-
 alpha-D-glucose alpha-D-glucose Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38500
-
 enzyme form II, sucrose density gradient centrifugation Sus scrofa
38800
-
 enzyme form III, sucrose density gradient centrifugation Sus scrofa
39000
-
 enzyme form II, sucrose density gradient centrifugation Sus scrofa
39100
-
 enzyme form IV, sucrose density gradient centrifugation Sus scrofa
41000
-
 1 * 41000, enzyme form I and II, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
 hog
-

Purification (Commentary)

Purification (Comment) Organism
multiple forms: I, II, III, and IV. Two major forms: I and II are purified Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney cortex Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-glucose
-
 Sus scrofa beta-D-glucose
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 41000, enzyme form I and II, SDS-PAGE Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 37 enzyme form I, II, III, and IV Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 enzyme form I, II, III, and IV Sus scrofa