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Literature summary extracted from

  • Wlodawer, A.; Li, M.; Gustchina, A.; Oyama, H.; Dunn, B.M.; Oda, K.
    Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases (2003), Acta Biochim. Pol., 50, 81-102.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.100
-
Pseudomonas sp.
3.4.21.101
-
Xanthomonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.100 Ca2+ Ca2+-binding site Pseudomonas sp.
3.4.21.101 Ca2+ Ca2+-binding site Xanthomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.B48 Bacillus novosp.
-
MN-32
-
3.4.21.B48 Bacillus novosp. MN-32
-
MN-32
-
3.4.21.100 Pseudomonas sp.
-
101
-
3.4.21.101 Xanthomonas sp.
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.21.100 proteolytic modification N-terminal propeptide Pseudomonas sp.
3.4.21.101 proteolytic modification N-terminal propeptide and C-terminal propeptide Xanthomonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.4.21.B48 KSCP
-
Bacillus novosp.
3.4.21.B48 kumamolysin
-
Bacillus novosp.
3.4.21.100 PSCP
-
Pseudomonas sp.
3.4.21.100 pseudomonapepsin
-
Pseudomonas sp.
3.4.21.100 Pseudomonas serine-carboxyl proteinase
-
Pseudomonas sp.
3.4.21.100 sedolisin
-
Pseudomonas sp.
3.4.21.101 sedolisin-B
-
Xanthomonas sp.
3.4.21.101 xanthomonapepsin
-
Xanthomonas sp.
3.4.21.101 Xanthomonas serine-carboxyl proteinase
-
Xanthomonas sp.
3.4.21.101 XSCP
-
Xanthomonas sp.