Literature summary for 3.5.1.11 extracted from

Hewitt, L.; Kasche, V.; Lummer, K.; Lewis, R.J.; Murshudov, G.N.; Verma, C.S.; Dodson, G.G.; Wilson, K.S.
Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft (2000), J. Mol. Biol., 302, 887-898.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapour diffusion at 18°C, crystal structure of a slowly processing precursor mutant T263G	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	the enzyme is a periplasmic protein, cytoplasmically expressed as a precursor polypeptide comprising a signal sequence, the A and B chains of the mature enzyme, 209 and 557 residues respectively, joined by a spacer peptide of 54 amino acid residues. The wild-type AB heterodimer is produced by proteolytic removal of this spacer in the periplasm	Escherichia coli	-	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the enzyme is a periplasmic protein, cytoplasmically expressed as a precursor polypeptide comprising a signal sequence, the A and B chains of the mature enzyme, 209 and 557 residues respectively, joined by a spacer peptide of 54 amino acid residues. The wild-type AB heterodimer is produced by proteolytic removal of this spacer in the periplasm. The first step in processing is believed to be autocatalytic hydrolysis of the peptide bond between the C-terminal residue of the spacer and the active-site serine residue at the N-terminus of the B chain. The crystal structure of a slowly processing mutant enzyme reveals that the spacer peptide blocks the entrance to the active site cleft consistent with an autocatalytic mechanism of maturation. For the slowly processed T263G mutant the crystal structure demonstrates a primary cleavage site between Tyr260 and Pro261. This must be followed by a cleavage between Gly263 and Ser264	Escherichia coli

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Release 2023.1 (January 2023)