3.4.23.32: Scytalidopepsin B

This is an abbreviated version!
For detailed information about Scytalidopepsin B, go to the full flat file.

Reaction

Hydrolysis of proteins with broad specificity, cleaving Phe24-/-Phe, but not Leu15-Tyr and Phe25-Tyr in the B chain of insulin =

Synonyms

eqolisin, Ganoderma lucidum carboxyl proteinase, More, Proteinase, Ganoderma lucidum aspartic, Proteinase, Scytalidium lignicolum aspartic, B, SCP-B, Scytalidium aspartic proteinase B, Scytalidium lignicolum pepstatin-insensitive carboxyl peptidase, Scytalido-carboxyl peptidase-B, scytalidoglutamic peptidase, SGP, SLB

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.32 Scytalidopepsin B

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Results	in table
1	AA Sequence
1	CAS Registry Number
1	Cloned(Commentary)
3	Crystallization (Commentary)
18	Inhibitors
28	kcat/KM [mM/s]
29	KM Value [mM]
1	Localization
2	Metals/Ions
6	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
16	Organism
5	PDB ID
7	pH Optimum
2	pH Range
10	pH Stability
1	pI Value
3	Posttranslational Modification
4	Protein Variants
3	Purification (Commentary)
3	Reaction
1	Reaction Type
16	Reference
4	Source Tissue
4	Specific Activity [micromol/min/mg]
58	Substrates and Products (Substrate)
4	Subunits
17	Synonyms
3	Temperature Optimum [°C]
1	Temperature Range [°C]
9	Temperature Stability [°C]
29	Turnover Number [1/s]

Engineering

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Engineering on EC 3.4.23.32 - Scytalidopepsin B

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D43A

Scytalidium lignicola

P15369

the mutant has approximately 20% of the original activity

753080

E136A

Scytalidium lignicola

-

mutant loses the ability for self-activation and cleavage of the propeptide. Mutant has no peptidase activity

685437

Q53A

Scytalidium lignicola

-

mutant loses the ability for self-activation and cleavage of the propeptide. Mutant has no peptidase activity

685437

Q53E

Scytalidium lignicola

-

mutant loses the ability for self-activation and cleavage of the propeptide. Mutant has no peptidase activity

685437