Information on EC 3.4.21.12 - alpha-lytic endopeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.12
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RECOMMENDED NAME
GeneOntology No.
alpha-lytic endopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential cleavage: Ala-/-, Val-/- in bacterial cell walls, elastin and other proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-76-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-Ala-Pro-Ala-4-nitroanilide + H2O
?
show the reaction diagram
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-
-
-
?
casein + H2O
?
show the reaction diagram
Elastin + H2O
?
show the reaction diagram
insulin + H2O
?
show the reaction diagram
N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
N-succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
show the reaction diagram
peptidoglycan + H2O
?
show the reaction diagram
succinyl-Ala-Ala-Pro-Ala-4-nitroanilide
?
show the reaction diagram
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-
-
?
succinyl-Ala-Ala-Pro-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Ala + 4-nitroanilide
show the reaction diagram
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high activity with wild-type enzyme and mutant enzyme M190A
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?
succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Leu + 4-nitroanilide
show the reaction diagram
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weak activity with wild-type enzyme, high activity with mutant enzyme M190A
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?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroanilide
show the reaction diagram
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weak activity with wild-type enzyme, high activity with mutant enzyme M190A
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?
succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Val + 4-nitroanilide
show the reaction diagram
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high activity with wild-type enzyme and mutant enzyme M190A
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?
succinyl-Ala-Ala-Pro-X-p-nitroanilide + H2O
?
show the reaction diagram
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X: Gly, Thr, Val, Leu, Ile, Met, Phe
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-
?
succinyl-Ala-Pro-Ala-p-nitroanilide + H2O
?
show the reaction diagram
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-
-
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?
tert-butyloxycarbonyl-Ala-p-nitrophenyl ester + H2O
?
show the reaction diagram
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-
-
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?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Eglin c
guanidine hydrochloride
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1% residual activity in the presence of 4 mM guanidine hydrochloride
methoxysuccinyl-Ala-Ala-Pro-L-boroPhe
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the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates close to tetrahedral boron coordination in the active site of the enzyme/inhibitor complex
methoxysuccinyl-Ala-Ala-Pro-L-boroVal
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the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates tetrahedral boron coordination in the active site of the enzyme/inhibitor complex
N-terminal 166 amino acid Pro region of alpha-lytic protease
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dual role of folding and inhibition
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N-Tert-butyloxycarbonylalanylpropylvaline boronic acid
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SDS
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42% residual activity in the presence of 1% (w/v) SDS
Turkey ovomucoid third domain
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Urea
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12% residual activity in the presence of 4 mM urea
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sodium deoxycholate
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196% activity in the presence of 0.1% (w/v) sodium deoxycholate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19870
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amino acid analysis
19910
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ion-spray mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure solved at 0.83 A resolution at pH 8
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subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
alpha-lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities
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kinetic stability impaired by the large, cooperative unfolding barrier plays a critical role in extending the lifetime of the protease in its harsh environment
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lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity
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Pro N-domain both provides direct interactions with alpha-lytic protease that stabilize the folding transition state and confers stability to the Pro C-domain
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of recombinant enzymes in Escherichia coli
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mutant enzyme precursor with a pro region lacking its last three amino acids: the turnover number of folding of the mutant enzyme is 1000fold lower that for the folding of the wild type enzyme. Mutant enzyme precursor with a pro region lacking its last three amino acids and two additional mutations, R102H and G134S: turnover number of folding of the mutant enzyme is 2fold higher than that of the wild-type enzyme
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G216A
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216D
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no active enzyme
G216F
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216G
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216H
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216I
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216K
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no active enzyme
G216L
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216N
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no active enzyme
G216P
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no active enzyme
G216Q
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216R
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no active enzyme
G216S
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216T
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216V
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216W
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216Y
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active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
additional information
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Pro region N-domain mutants: disruption of the hydrogen bonding potentials of Y26 and E30 primarily alters Pro binding to the folding transition state as compared to binding in the initial and native state complexes