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Literature summary for 5.2.1.8 extracted from

  • Sheldon, P.S.; Venis, M.A.
    Purification and characterization of cytosolic and microsomal cyclophilins from maize (Zea mays) (1996), Biochem. J., 315, 965-969.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
about 80% of activity is lost on freezing the purified microsomal enzyme in liquid N2 and thawing Zea mays

Inhibitors

Inhibitors Comment Organism Structure
cyclosporin A inhibits cytosolic and microsomal enzyme form Zea mays
NEM cytosolic enzyme form Zea mays
Phenylglyoxal cytosolic enzyme form Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Zea mays 5829
-
microsome
-
Zea mays
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
11000 16000 cytosolic enzyme form, gel filtration on various matrices Zea mays
17500
-
1 * 17500, cytosolic enzyme form, SDS-PAGE Zea mays
17700
-
1 * 17700, microsomal enzyme form, SDS-PAGE Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
shoot etiolated Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Zea mays

Subunits

Subunits Comment Organism
monomer 1 * 17700, microsomal enzyme form, SDS-PAGE Zea mays
monomer 1 * 17500, cytosolic enzyme form, SDS-PAGE Zea mays