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Literature summary for 3.4.23.4 extracted from

  • van den Brink, H.J.; Petersen, S.G.; Rahbek-Nielsen, H.; Hellmuth, K.; Harboe, M.
    Increased production of chymosin by glycosylation (2006), J. Biotechnol., 125, 304-310.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
S351T mutant of prochymosin as fusion protein with the Aspergillus niger enzyme glucoamylase in Aspergillus niger var. awamori, insertion of a short peptide linker between the proteins with the sequence TDNST Bos taurus

Protein Variants

Protein Variants Comment Organism
S351T insertion of a glycosylation site in the linker region between chymosin and glucoamylase, strongly improves enzyme secretion Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
kappa-casein + H2O Bos taurus cleaves a single bond between phenylalanine 105 and methionine 106 ?
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
use of a synthetic gene that encodes a protein identical to bovine prochymosin
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information insertion of a glycosylation site (S351T), glycosylation has significant inhibitory effect but this can be circumvented by deglycosylation with endoglucosidase H Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
kappa-casein + H2O cleaves a single bond between phenylalanine 105 and methionine 106 Bos taurus ?
-
?