3.4.24.40: serralysin

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

Reaction

Preferential cleavage of bonds with hydrophobic residues in P1' =

Synonyms

aeruginolysin, Alkaline protease, AMP-P, AP, APR, AprA, AprX, arazyme, calcium-regulated alkaline protease, DR2310 protease, Escherichia freundii proteinase, Extracellular metalloproteinase, LupA, More, protease B, protease C, protease I, Proteinase, Serratia marcescens metallo-, PrtA, PrtA metalloprotease, PrtC, pseudomonal serralysin, Pseudomonas aeruginosa alk. protease, Pseudomonas aeruginosa alkaline protease, Pseudomonas aeruginosa alkaline proteinase, Pseudomonas alkaline protease, psychrophilic alkaline metalloprotease, serralysin, serralysin-like metalloprotease, Serratia marcescens extracellular proteinase, Serratia marcescens metalloprotease, Serratia marcescens metalloproteinase, SlpB, SMP, thermoalkaline protease, thermostable alkaline protease, zinc proteinase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.40 serralysin

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Results	in table
1	Activating Compound
1130	AA Sequence
4	Application
1	CAS Registry Number
16	Cloned(Commentary)
9	Crystallization (Commentary)
2	Expression
8	General Information
2	General Stability
176	Inhibitors
36	kcat/KM [mM/s]
12	Ki Value [mM]
77	KM Value [mM]
37	Localization
89	Metals/Ions
49	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
74	Organism
13	PDB ID
34	pH Optimum
9	pH Range
12	pH Stability
3	pI Value
1	Posttranslational Modification
13	Protein Variants
29	Purification (Commentary)
1	Reaction
1	Reaction Type
72	Reference
1	Renatured (Commentary)
12	Source Tissue
10	Specific Activity [micromol/min/mg]
4	Storage Stability
261	Substrates and Products (Substrate)
19	Subunits
64	Synonyms
15	Temperature Optimum [°C]
3	Temperature Range [°C]
25	Temperature Stability [°C]
48	Turnover Number [1/s]

Engineering

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Engineering on EC 3.4.24.40 - serralysin

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

M226A

Dickeya chrysanthemi

-

using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants

707612

M226A/E189A

Dickeya chrysanthemi

-

introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain

707612

M226H

Dickeya chrysanthemi

-

mutant could not be purified, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants

707612

M226H/E189A

Dickeya chrysanthemi

-

introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain

707612

M226I

Dickeya chrysanthemi

-

M226I possesses 50% of wild-type activity, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants

707612

M226I/E189A

Dickeya chrysanthemi

-

introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain

707612

M226L

Dickeya chrysanthemi

-

M226L possesses 85% of wild-type activity, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants

707612

M226L/E189A

Dickeya chrysanthemi

-

introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain

707612

M226N

Dickeya chrysanthemi

-

mutant could not be purified

707612

M226N/E189A

Dickeya chrysanthemi

-

introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain

707612

additional information

3 entries

additional information

Pseudomonas aeruginosa

-

enzyme form bearing residues Leu-Lys at the N-terminus, in the absence of calcium far more efficient degradation of interleukins IL-6 and IL-8 than wild-type

667880

additional information

Pseudomonas aeruginosa

-

recombinant protein labeled with L-difluoromethionine in invariant position of M214 shows little effect on protein structure or function

668081

additional information

Pseudomonas aeruginosa

-

generation of a series of full-length and truncation mutants for structural and functional studies, overview. DELTAN-AP shows increased thermal sensitivity compared with the wild-type enzyme. At 42°C, protease activity decreases by 50%, and at 55°C, protease activity decreases by 90% when compared with the full-length AP in 2 mM Ca2+

717874