3.4.24.70: oligopeptidase A

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For detailed information about oligopeptidase A, go to the full flat file.

Reaction

hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but additional information distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5 =

Synonyms

68000-M Signalpeptide hydrolase, More, oligopeptidase A, OpdA, prlC, TOP, Top1, Top2

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.70 oligopeptidase A

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Results	in table
13052	AA Sequence
2	CAS Registry Number
14	Cloned(Commentary)
1	Cofactor
1	Crystallization (Commentary)
1	Expression
7	General Information
23	Inhibitors
14	kcat/KM [mM/s]
15	KM Value [mM]
6	Localization
18	Metals/Ions
4	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
62	Organism
1	PDB ID
3	pH Optimum
1	pH Range
3	Protein Variants
10	Purification (Commentary)
2	Reaction
1	Reaction Type
60	Reference
1	Source Tissue
5	Specific Activity [micromol/min/mg]
1	Storage Stability
57	Substrates and Products (Substrate)
3	Subunits
57	Synonyms
6	Temperature Optimum [°C]
14	Turnover Number [1/s]

Engineering

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Engineering on EC 3.4.24.70 - oligopeptidase A

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Y607A

Escherichia coli

-

the mutant shows altered substrate and cleavage site specificity compared to the wild-type enzyme, structure comparison with the wild-type enzyme, overview. The mutant is highly activated by NaCl in contrast to the wild-type enzyme

707285

Y607F

Escherichia coli

-

the mutant shows altered substrate and cleavage site specificity compared to the wild-type enzyme, structure comparison with the wild-type enzyme, overview. The mutant is highly activated by NaCl in contrast to the wild-type enzyme

707285

additional information

Escherichia coli

-

supressors of the protein-localization defect conferred by certain signal sequence mutations

668829