3.4.21.B54: Pyrococcus abyssi serine endopeptidase

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For detailed information about Pyrococcus abyssi serine endopeptidase, go to the full flat file.

Reaction

high affinity for aromatic (Phe and Tyr) and hydrophobic amino acids (mainly Leu) in P1 position, specificity for aromatic moieties in P1' position =

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.B54 Pyrococcus abyssi serine endopeptidase

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Results	in table
1	General Stability
8	Inhibitors
1	Molecular Weight [Da]
2	Organism
1	pH Optimum
1	pH Range
1	Purification (Commentary)
1	Reaction
2	Reference
6	Substrates and Products (Substrate)
2	Subunits
1	Temperature Optimum [°C]
1	Temperature Range [°C]
4	Temperature Stability [°C]

Substrates Products

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Substrates Products on EC 3.4.21.B54 - Pyrococcus abyssi serine endopeptidase

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SUBSTRATE

PRODUCT                       

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

Reversibility
r=reversible
ir=irreversible
?=not specified

oxidized insulin B-chain + H2O

oxidized insulin B-chain peptide fragments

2 entries

succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O

succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline

2 entries

succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O

succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline

2 entries

oxidized insulin B-chain + H2O

oxidized insulin B-chain peptide fragments

Pyrococcus abyssi

-

high affinity for aromatic (Phe and Tyr) and hydrophobic amino acids (mainly Leu) in P1 position, specificity for aromatic moieties in P1' position

722254

-

-

?

oxidized insulin B-chain + H2O

oxidized insulin B-chain peptide fragments

Pyrococcus abyssi st 549

-

high affinity for aromatic (Phe and Tyr) and hydrophobic amino acids (mainly Leu) in P1 position, specificity for aromatic moieties in P1' position

722254

-

-

?

succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O

succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline

Pyrococcus abyssi

-

protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed

722254

-

-

?

succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O

succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline

Pyrococcus abyssi st 549

-

protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed

722254

-

-

?

succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O

succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline

Pyrococcus abyssi

-

protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed

722254

-

-

?

succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O

succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline

Pyrococcus abyssi st 549

-

protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed

722254

-

-

?