3.4.11.B7: arginyl aminopeptidase PH1704

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For detailed information about arginyl aminopeptidase PH1704, go to the full flat file.

Reaction

the enzyme is an aminopeptidase with limited specificity, mainly releasing the N-terminal L-arginine and hardly cleaving other amino acids. L-Arg-7-amido-4-methylcoumarin is the best artificial substrate =

Synonyms

arginine-specific aminopeptidase, PH1704, PH1704 protease

ECTree

3 Hydrolases

3.4 Acting on peptide bonds (peptidases)

3.4.11 Aminopeptidases

3.4.11.B7 arginyl aminopeptidase PH1704

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Results	in table
1	AA Sequence
1	Cloned(Commentary)
1	Crystallization (Commentary)
1	Inhibitors
2	Localization
10	Metals/Ions
2	Molecular Weight [Da]
12	Organism
1	pH Optimum
5	Protein Variants
2	Purification (Commentary)
1	Reaction
6	Reference
18	Substrates and Products (Substrate)
5	Subunits
8	Synonyms
1	Temperature Optimum [°C]
1	Temperature Stability [°C]

Engineering

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Engineering on EC 3.4.11.B7 - arginyl aminopeptidase PH1704

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E12T

Pyrococcus horikoshii

O59413

protease activity of E12T is 3.8 fold higher than that of wild-type enzyme. The mutant is more stable than wild-type at 85°C

709586

Y120P

Pyrococcus horikoshii

O59413

kat and kat/Km of the mutant enzyme with L-Arg-7-amino-4-methylcoumarin are about 7 and 7.8times higher than that of the wild type enzyme, respectively

730765

E12T

Pyrococcus horikoshii DSM 12428

protease activity of E12T is 3.8 fold higher than that of wild-type enzyme. The mutant is more stable than wild-type at 85°C

Y120P

2 entries