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Literature summary extracted from

  • Leon, J.; Vega, J.M.
    Effect of immobilization on the kinetic ans stability properties of o-acetyl-L-serine sulfhydrylase from Chlamydomonas reinhardtii (1992), Biocatalysis, 7, 29-35.
No PubMed abstract available

Application

EC Number Application Comment Organism
2.5.1.47 synthesis synthesis of L-Cys, therefore immobilization Chlamydomonas reinhardtii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.47 additional information
-
 additional information not significantly altered by immobilization Chlamydomonas reinhardtii

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Chlamydomonas reinhardtii
-
-
-

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.47 50
-
 soluble enzyme, DEAE-immobilized enzyme and silica-immobilized enzyme Chlamydomonas reinhardtii
2.5.1.47 60
-
 vinylacetate-epoxy-immobilized enzyme and vinylacetate-hydroxy-immobilized enzyme Chlamydomonas reinhardtii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.47 70
-
 10 min, 10% loss of activity of immobilized enzyme, 65-80% loss of activity of native enzyme Chlamydomonas reinhardtii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.5.1.47 additional information
-
 altered by immobilization Chlamydomonas reinhardtii