3.4.11.B4: Pyrococcus horikoshii deblocking aminopeptidase

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Reaction

The enzyme exhibits aminopeptidase activity and with lower efficiency deblocking activity (i.e. hydrolysis of acetylated amino acids from the N-terminus of peptides). The turnover number with Ac-Ala-Ala-Ala is 260-540fold lower compared to the activity with Ala-Ala-Ala. The turnover number with Ac-Ala-Ala is 350fold lower compared to the activity with Ala-Ala. Low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme is activated by Co2+ or Zn2+. Contains 1.32 mol of Ca2+ per mol of monomer. =

Synonyms

DAP1, DAP2, DAP3, DAPPh, DAPPh2, DAPPh3, deblocking aminopeptidase, PH0519, PH1527, PH1821

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.11 Aminopeptidases

                3.4.11.B4 Pyrococcus horikoshii deblocking aminopeptidase

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Results	in table
3	AA Sequence
4	Cloned(Commentary)
1	Crystallization (Commentary)
1	General Information
2	Inhibitors
8	KM Value [mM]
6	Metals/Ions
6	Molecular Weight [Da]
7	Organism
3	pH Optimum
3	pH Range
3	Protein Variants
4	Purification (Commentary)
1	Reaction
4	Reference
17	Substrates and Products (Substrate)
4	Subunits
19	Synonyms
4	Temperature Optimum [°C]
3	Temperature Range [°C]
4	Temperature Stability [°C]
9	Turnover Number [1/s]

Engineering

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D173N

Pyrococcus horikoshii

O58255

Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced

718729

E205Q

Pyrococcus horikoshii

O58255

Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced

718729

E206Q

Pyrococcus horikoshii

O58255

Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced

718729