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Literature summary for 3.2.1.166 extracted from

  • Nasser, N.J.; Nevo, E.; Shafat, I.; Ilan, N.; Vlodavsky, I.; Avivi, A.
    Adaptive evolution of heparanase in hypoxia-tolerant Spalax: gene cloning and identification of a unique splice variant (2005), Proc. Natl. Acad. Sci. USA, 102, 15161-15166.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.166

Protein Variants

Protein Variants Comment Organism
additional information a splice variant of the Spalax enzyme lacking 16 aa encoded by exon 7. This deletion results in a major defect in trafficking and processing of the heparanase protein, leading to a loss of its enzymatic activity Nannospalax judaei

Organism

Organism UniProt Comment Textmining
Nannospalax galili
-
-
-
Nannospalax judaei Q333X5
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Nannospalax judaei
-
brain
-
 Nannospalax galili
-
eye
-
 Nannospalax judaei
-
heart
-
 Nannospalax judaei
-
kidney
-
 Nannospalax judaei
-
kidney
-
 Nannospalax galili
-
liver
-
 Nannospalax judaei
-
liver
-
 Nannospalax galili
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heparan sulfate proteoglycan + H2O heparanase results in release of low-molecular-weight-labeled degradation fragments. The degradation products of heparan sulfate are 5- to 6fold smaller than intact HS side chains Nannospalax judaei heparan sulfate fragment + truncated heparan sulfate proteoglycan
-
 ?
heparan sulfate proteoglycan + H2O heparanase results in release of low-molecular-weight-labeled degradation fragments. The degradation products of heparan sulfate are 5- to 6fold smaller than intact HS side chains Nannospalax galili heparan sulfate fragment + truncated heparan sulfate proteoglycan
-
 ?