Literature summary for 3.4.22.65 extracted from

Shoji, H.; Shibuya, I.; Hirai, M.; Horiuchi, H.; Takagi, M.
Production of recombinant Der f1 with the native IgE-binding activity using a baculovirus expression system (1997), Biosci. Biotechnol. Biochem., 61, 1668-1673.

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant Der f1 that is produced using a baculovirus expression sytem contains pro-sequences of different length. Most of theses can be removed by acid treatment. The N-terminal amino acids of the acid-treated recombinant enzyme are uniform. A method for processing of the pro-sequence has been developed by producing reDer f1 E(-1)K with baculovirus expression system in which the carboxy terminal amino acid of the pro-sequence (glutamate) is replaced by lysine. Addition of lysylendopeptidase into the culture medium leads to processing of the pro-sequence of reDer f1 E(-1)K	Dermatophagoides farinae

Cloned (Comment)

Organism

recombinant Der f1 that is produced using a baculovirus expression sytem contains pro-sequences of different length. Most of theses can be removed by acid treatment. The N-terminal amino acids of the acid-treated recombinant enzyme are uniform. A method for processing of the pro-sequence has been developed by producing reDer f1 E(-1)K with baculovirus expression system in which the carboxy terminal amino acid of the pro-sequence (glutamate) is replaced by lysine. Addition of lysylendopeptidase into the culture medium leads to processing of the pro-sequence of reDer f1 E(-1)K

Dermatophagoides farinae

Protein Variants

Protein Variants	Comment	Organism
additional information	lysylendopeptidase-treated reDER f1 E(-1)K shows some differences in protease activity and reactivity with lectins: GlcNAc is contained at the non-reducing terminus of the sugar chains of native Der f1 but not of lysylendopeptidase-treated reDEr f1 E(-1)K. Lysylendopeptidase-treated reDEr f1 E(-1)K reacts with Lens culinaris agglutinin but native Der f1 does not, suggesting that fucose is connected with GlcNAc, bound to an asparagine residue, but not of native Der f1. Their N-terminal amino acid and the IgE-binding activity are the same as those of the native one	Dermatophagoides farinae

Organism

Organism	UniProt	Comment	Textmining
Dermatophagoides farinae	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	GlcNAc is contained at the non-reducing terminus of the sugar chains of native Der f1 but not of lysylendopeptidase-treated reDEr f1 E(-1)K. Lysylendopeptidase-treated reDEr f1 E(-1)K reacts with Lens culinaris agglutinin but native Der f1 does not , suggesting that fucose is connected with GlcNAc, bound to an asparagine residue, but not of native Der f1	Dermatophagoides farinae