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Information on EC 3.4.21.97 - assemblin
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3.4.21.97 assemblinSpecify your search results
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- 3.4.21.97
- viruses
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genital
- acyclovir
- infectious
- women
- ganglia
- transmitted
- virion
- thymidine
- encephalitis
- plaque
- corneal
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trigeminal
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ocular
- herpesviruses
- keratitis
- igg
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herpetic
- vaginal
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seropositive
- immunodeficiency
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serological
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immediate-early
- type-1
- ulcer
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seroprevalence
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type-specific
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lytic
-
epstein-barr
- chlamydia
- tegument
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neurotropic
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cytopathic
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oncolytic
- syphilis
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intravaginal
-
swab
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postinfection
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virus-specific
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microbicide
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replication-defective
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seronegative
- co-infection
- ganciclovir
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superinfect
- pseudorabies
-
mucocutaneous
- analysis
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intercourse
- medicine
-
heterosexual
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cervicovaginal
The enzyme appears in viruses and cellular organisms
Synonyms
hsv-1, hsv-2, assemblin, hcmv protease, hsv-1 protease, human cytomegalovirus protease, capsid scaffolding protein, cytomegalovirus protease, hhv-6 proteinase, pul80a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Assemblin
assembly protein precursor-processing proteinase
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capsid scaffolding protein
cytomeglovirus protease
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-
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Herpes simplex virus 1 proteinase Pra
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Herpes simplex virus endopeptidase
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HHV-6 proteinase
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hMCV
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HSV 1 protease
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HSV-1
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HSV-2
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human cytomegalovirus maturational proteinase
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human cytomegalovirus protease
human cytomegalovirus proteinase
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proteinase, assembly protein precursor-processing
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SFA
Varicella-zoster virus gene 33 proteinase
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Assemblin
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human cytomegalovirus protease
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleaves -Ala-/-Ser- and -Ala-/-Ala- bonds in the scaffold protein
Involved in the breakdown of the scaffold protein during the late stages of assembly of the herpes-virus virion. Inhibited by diisopropyl fluorophosphate. Type example of peptidase family S21. Catalytic residues are His, Ser, His, a combination not known for any other peptidase, and the protein fold also is unique. Known from herpes viruses of several types, cytomegalovirus, Epstein-Barr virus and human herpesvirus 3.
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Cleaves -Ala-/-Ser- and -Ala-/-Ala- bonds in the scaffold protein
serine protease that operates by an induced-fit mechanism
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CAS REGISTRY NUMBER
COMMENTARY
139691-88-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid + H2O
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNA + S-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
-
-
-
?
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid + H2O
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNA + Ser-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
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-
-
-
?
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid + H2O
?
-
-
-
-
?
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNASSRLA-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid + H2O
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNA + SSRLA-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
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-
-
?
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala((2'-aminoethyl)amino-naphthalene-1)sulfonic acid + H2O
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala + Ser-Ser-Arg-Leu-Ala((2'-aminoethyl)amino-naphthalene-1)sulfonic acid
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-
-
?
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid + H2O
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala + Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala + Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
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-
-
?
Abz-GVVNASSRLAY(NO2)G + H2O
anthranilamide-GVVNA + SSRLAY(NO2)G
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-
-
?
Abz-VVNASSLY(3-NO2)R-OH + H2O
Abz-VVNA + SSLY(3-NO2)R-OH
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-
-
?
acetyl-Cys-tert-butylglycine-tert-butylglycine-Asn(Me)2-Ala-7-amido-4-methylcoumarin + H2O
acetyl-Cys-tert-butylglycine-tert-butylglycine-Asn(Me)2-Ala + 7-amino-4-methylcoumarin
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-
-
?
acetyl-L-Gln-L-Ala-gancyclovir + H2O
acetyl-L-Gln-L-Ala + ganciclovir
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dipeptide prodrugs of ganciclovir
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?
assembly protein precursor of cytomegalovirus + H2O
?
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the enzyme is essential for virus replication and functions during capsid assembly from pAP, i.e. assembly protein precursor
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?
biotinyl-RGVVNASSRLAK-fluorescein isothiocyanate + H2O
biotinyl-RGVVNA + SSRLAK-fluorescein isothiocyanate
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?
cytomegalovirus assembly protein precursor + H2O
?
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cleavage at the C-terminal maturation site, i.e. M-site, between Ala643-Ser644, autoproteolytic cleavage at the R-site between Ala256-Ser257, internal cleavage sites, i.e. I-sites are Ala143-Ala144, Ala209-Ser210, cleavage occurs at the M-site first, followed by the R-site and then the I-sites
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?
N-(5'-phosphoribosyl)anthranilate isomerase + H2O
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site-specific cleavage and functional inactivation of the N-(5'-phosphoribosyl)anthranilate isomerase, thereby leading to an arrest of cell proliferation. Coexpressing N-(5'-phosphoribosyl)anthranilate isomerase1194-M with the protease exhibits a growth reduction of 35%. N-(5'-phosphoribosyl)anthranilate isomerase1132-M- as well as N-(5'-phosphoribosyl)anthranilate isomerase1165-M-expressing cells do not show growth reduction upon coexpressing HCMV protease, thus no cleavage occurs. Cells expressing the modified N-(5'-phosphoribosyl)anthranilate isomerase1194-Me together with the active protease show 85% reduction of cell proliferation, is cleaved in a sequence-specific manner
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?
pPR + H2O
?
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one substrate used in this study is pPR itself inactivated by replacing its catalytic nucleophile (S132A)
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?
simian cytomegalovirus precursor assembly protein + H2O
assembly protein
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assemblin and its precursor, pPR, have comparable enzymatic activities
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?
succinyl-LVNAS-2-aminobutyryl-Arg-NH2 + H2O
succinyl-LVNA + Ser-2-aminobutyryl-Arg-NH2
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-
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?
succinyl-LVNAS-2-aminobutyryl-EPT-NH2
succinyl-LVNA + S-2-aminobutyryl-EPT-NH2
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-
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?
succinyl-LVNAS-2-aminobutyryl-EPT-NH2 + H2O
succinyl-LVNA + Ser-2-aminobutyryl-EPT-NH2 + H2O
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-
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-
?
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid + H2O
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala + Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
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-
-
?
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid + H2O
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala + Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
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studies of substrate-induced conformational changes in human cytomegalovirus protease using optical biosensor technology
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?
RGVVNASSRLAK + H2O
RGVVNA + SSRLAK
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substrate mimicking M-site substrate
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?
succinyl-RRYIKASEPPV-NH2 + H2O
succinyl-RRYIKA + SEPPV-NH2
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?
succinyl-VVNAS-2-aminobutyryl-R-NH2 + H2O
succinyl-VVNA + S-2-aminobutyryl-R-NH2
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?
succinyl-VVNAS-2-aminobutyryl-R-NH2 + H2O
succinyl-VVNA + S-2-aminobutyryl-R-NH2
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?
SYVKASVSPE + H2O
SYVKA + SVSPE
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substrate mimicking R-site substrate
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?
additional information
?
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the production of infectious cytomegalovirus requires neither I-site cleavage of assemblin nor the presence of assemblin in mature virion
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
assembly protein precursor of cytomegalovirus + H2O
?
-
the enzyme is essential for virus replication and functions during capsid assembly from pAP, i.e. assembly protein precursor
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?
pPR + H2O
?
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one substrate used in this study is pPR itself inactivated by replacing its catalytic nucleophile (S132A)
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?
additional information
?
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the production of infectious cytomegalovirus requires neither I-site cleavage of assemblin nor the presence of assemblin in mature virion
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-[[(3aS,6S,6aR)-4-(1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00018 mM
(2S)-2-[[(3aS,6S,6aR)-4-(4-chloro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00029 mM
(2S)-2-[[(3aS,6S,6aR)-4-(4-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00024 mM
(2S)-2-[[(3aS,6S,6aR)-4-(4-methoxy-7-methyl-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]-pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.0011 mM
(2S)-2-[[(3aS,6S,6aR)-4-(5-chloro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00046 mM
(2S)-2-[[(3aS,6S,6aR)-4-(5-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00023 mM
(2S)-2-[[(3aS,6S,6aR)-4-(5-methoxy[1,3]thiazolo[5,4-b]-pyridin-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00087 mM
(2S)-2-[[(3aS,6S,6aR)-4-(6-ethylcarboxylate-1,2-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]-pyrrol-1(2H)yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00035 mM
(2S)-2-[[(3aS,6S,6aR)-4-(6-fluoro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00036 mM
(2S)-2-[[(3aS,6S,6aR)-4-(6-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00022 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-meth-yl5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropoxyphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00018 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(1-naphthyl)pyrrolidine-1-carboxamide
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IC50: 0.00065 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(2-isopropylphenyl)pyrrolidine-1-carboxamide
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0.00047 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(3-chlorophenyl)pyrrolidine-1-carboxamide
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IC50: 0.0014 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-chlorophenyl)pyrrolidine-1-carboxamide
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IC50: 0.00026 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.0002 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-propoxyphenyl)pyrrolidine-1-carboxamide
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IC50: 0.00021 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-[3-(trifluoromethyl)phenyl]pyrrolidine-1-carboxamide
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0.00059 mM
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-[4-(trifluoromethyl)phenyl]pyrrolidine-1-carboxamide
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IC50: 0.00023 mM
(2S)-2-[[(3aS,6S,6aR)-4-[(-cis-2,3-dimethylcyclopropyl)-cis-carbonyl]-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
(2S)-2-[[(3aS,6S,6aR)-4-[(-cis-2,3-dimethylcyclopropyl)-cis-carbony]-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.0003 mM
(2S)-2-[[(3aS,6S,6aR)-4-[(-cis-2,3-dimethylcyclopropyl)-trans-carbonyl]-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
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IC50: 0.0018 mM
(2S)-2-[[(3aS,6S,6aR)-4-[5-[(difluoromethyl)sulfonyl]-1,3-benzothiazol-2-yl]-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)-pyrrolidine-1-carboxamide
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IC50: 0.00021 mM
(2S)-2-[[(3aS,6S,6aR)-4-[6-(hydroxymethyl)-1,3-benzothiazol-2-yl]-6-methyl-5-oxohexahydropyrrolo[3,2-b]-pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
IC50: 0.00031 mM
(2S)-2-[[(3aS,6S,6aR)-6-methyl-4-(4-nitrophenyl)-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
IC50: 0.0087 mM
(2S)-2-[[(3aS,6S,6aR)-6-methyl-4-(6-nitro-1,3-benzothiazol-2-yl)-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
IC50: 0.00039 mM
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-(1,3-thiazol-2-yl)hexahydropyrrolo[3,2-b]pyrrol-1(2H)yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
IC50: 0.0015 mM
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-[(2,2,3,3-tetramethylcyclopropyl)carbonyl]hexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
IC50: above 0.02 mM
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-[1,3]thiazolo-[5,4-b]pyridin-2-ylhexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
IC50: 0.00029 mM
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-[6-(trifluoromethoxy)-1,3-benzothiazol-2-yl]hexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
IC50: 0.00046 mM
(3aR,6R,6aS)-4-Acetyl-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 1 mM
(3aS,6S,6aR)-4-(2-Etoxy-acetyl)-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.006 mM
(3aS,6S,6aR)-4-Acetyl-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.11 mM; IC50: 0.79 mM
(3R,3aS,6aR)-1-Acetyl-3-methyl-4-([(2S)-1-[(4-methylphenyl) sulfonyl]pyrrolidin-2-yl]carbonyl)hexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: 0.159 mM
(3R,3aS,6aR)-1-Acetyl-4-[((2S)-1-[[5-(dimethylamino)-1-naphthyl] sulfonyl]pyrrolidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: above 0.5 mM
(3R,3aS,6aR)-1-Acetyl-4-[[(2S)-1-benzoylpyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: above 0.5 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-(2-naphthylsulfonyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: below 0.00019 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-(1-naphthylsulfonyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.00037 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-(4-propoxybenzoyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.00054 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-[(4-propoxyphenyl)sulfonyl]pyrrolidin-2-yl]-carbonyl]hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.00023 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)1-(phenylsulfonyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.0018 mM
(3S,3aR,6aS)-1-(Cyclopropylcarbonyl)-4-([(2S)-1-[(3-isopropoxyphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: 0.065 mM
(3S,3aR,6aS)-1-(Cyclopropylcarbonyl)-4-[((2S)-1-[[5-(dimethylamino)-1-naphthyl]sulfonyl]pyrrolidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: 0.00034 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-(4-isopropylbenzoyl)pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)
-
IC50: 0.00039 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[(3-isopropoxyphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.065 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[(4-isopropoxyphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.0004 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[(4-isopropylphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.00046 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[[5-(dimethylamino)-1-naphthyl]sulfonyl]pyrrolidin-2-yl]-carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.00034 mM
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[[6-(dimethylamino)-1-naphthyl]sulfonyl]pyrrolidin-2-yl]-carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.0011 mM
(3S,3aR,6aS)-1-Acetyl-3-methyl-4-([(2S)-1-[(4-methylphenyl) sulfonyl]pyrrolidin-2-yl]carbonyl)hexahydropyrrolo-[3,2-b]pyrrol-2-one
-
IC50: 0.014 mM
(3S,3aR,6aS)-1-Acetyl-4-[((2S)-1-[[5-(dimethylamino)-1-naphthyl] sulfonyl]pyrrolidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.00054 mM
(3S,3aR,6aS)-1-Acetyl-4-[[(2S)-1-benzoylpyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.05 mM
(3S,3aR,6aS)-4-[[(2S)-1-(1,1'-biphenyl-4-ylcarbonyl)-pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.0003 mM
(3S,3aR,6aS)-4-[[(2S)-1-(4-chlorobenzoyl)pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-1(2H)-one
-
IC50: 0.0014 mM
(3S,3aR,6aS)-4-[[(2S)-1-(benzylsulfonyl)pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.0021 mM
(3S,3aR,6aS)-4-[[(2S)-1-[(4-chlorophenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: 0.00084 mM
(3S,3aR,6aS)-4-[[(2S)-1-[(5-chloro-3-methyl-1-benzothien-2-yl)carbonyl]pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2]pyrrol-2(1H)-one
-
IC50: 0.00019 mM
2-[2-(3,3-Dimethyl-butanoylamino)-3,3-dimethyl-butanoylamino]-N4,N4-dimethyl-N1-(1-methyl-2-oxo-propyl)-succinamide
-
-
2-[2-(3,3-Dimethyl-butanoylamino)-3,3-dimethyl-butanoylamino]-N4,N4-dimethyl-N1-(3,3,3-trifluoro-1-methyl-2-oxo-propyl)-succinamide
-
-
2-[2-(3,3-Dimethyl-butanoylamino)-3,3-dimethyl-butanoylamino]-N4,N4-dimethyl-N1-(3,3,4,4,4-pentafluoro-1-methyl-2-oxo-butyl)-succinamide
-
-
3-[((2S)-2-[[(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]pyrrolidin-1-yl)sulfonyl]-N,N-dimethylbenzamide
-
IC50: 0.00014 mM
3-[[((2S)-2-[[(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-carbonyl]pyrrolidin-1-yl)sulfonyl]methyl]-N,N-dimethylbenzamide
-
IC50: 0.0022 mM
4-(2-Etoxy-acetyl)-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.013 mM
BI31
-
50% inhibitory at 0.0017 mM. Increasing inhibitor concentrations in cells expressing the active protease correlate with increasing cell proliferation
BI36
-
50% inhibitory at 0.0005 mM. Increasing inhibitor concentrations in cells expressing the active protease correlate with increasing cell proliferation
monobactam inhibitors
-
beta-lactam derivatives with a carbon side-chain at C4 and a urea function at N1
-
N-[(1S)-2-[rel-(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-1-methyl-2-oxoethyl]-5-(dimethylamino)naphthalene-1-sulfonamide
-
IC50: 0.007 mM
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
N-[2-[rel-(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-2-oxoethyl]-5-(dimethylamino)-N-methylnaphthalene-1-sulfonamide
-
IC50: above 0.1 mM
N1-(2-Benzylcarbamoyl-1-methyl-2-oxo-ethyl)-2-[2-(3,3-dimethyl-butanoylamino)-3,3-dimethyl-butanoylamino]-N4,N4-dimethyl-succinamide
-
-
rel-(3aS,6R,6aR)-3-methyl-2-oxo-hexahydro-pyrrolo-[3,2-b]pyrrolo-1,4-dicarboxylic acid 4-benzyl ester 1-methyl ester
-
0.5 mM, 7.9% inhibition after 15 min
rel-(3aS,6R,6aR)-4-acetoxyacetyl-6-methyl-5-oxohexahydro-pyrrolo[3,2-b]pyrrolo-1-carboxylic acid benzyl ester
-
IC50: 0.805 mM
rel-(3aS,6R,6aR)-4-acetyl-6-methyl-5-oxo-hexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 1.8 mM, 0.5 mM, 15.4% inhibition after 15 min
rel-(3aS,6R,6aR)-4-methanesulfonyl-6-methyl-5-oxohexahydro-pyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
0.5 mM, 15% inhibition after 15 min
rel-(3aS,6S,6aR)-4-(2,2-Dimethylpropanoyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3aS,6S,6aR)-4-(2,4-Dinitrophenyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3aS,6S,6aR)-4-(2-Hydroxy-3-phenoxypropyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3aS,6S,6aR)-4-(3-Hydroxypropanoyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.133 mM
rel-(3aS,6S,6aR)-4-(4-Methoxybenzoyl)-6-methyl-5-oxohexahydropyrrolo [3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3aS,6S,6aR)-4-(Bicyclo[4.2.0]octa-1,3,5-trien-7-ylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.0115 mM
rel-(3aS,6S,6aR)-4-(cis-2,3-Dimethylcyclopropanecarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.072 mM
rel-(3aS,6S,6aR)-4-(cyclobutylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.032 mM
rel-(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.009 mM
rel-(3aS,6S,6aR)-4-(Dimethoxyphosphoryl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3aS,6S,6aR)-4-(Hydroxymethyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3aS,6S,6aR)-4-(trans-2,3-Dimethylcyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.1 mM
rel-(3aS,6S,6aR)-4-Formyl-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.398 mM
rel-(3aS,6S,6aR)-4-Isobutyryl-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.126 mM
rel-(3aS,6S,6aR)-6-Methyl-4-(methylthio)-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3aS,6S,6aR)-6-Methyl-4-[(2-methylcyclopropyl)-carbonyl]-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.01 mM
rel-(3aS,6S,6aR)-6-Methyl-5-oxo-4-(1H-pyrrol-1-ylcarbonyl)-hexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: 0.25 mM
rel-(3aS,6S,6aR)-6-Methyl-5-oxo-4-(2,2,3,3-tetramethylcyclopropylcarbonyl) hexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3aS,6S,6aR)-6-Methyl-5-oxo-4-[(1E)-3-oxobut-1-enyl]-hexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
-
IC50: above 0.5 mM
rel-(3S,3aR,6aS)-1-(Cyclopropylcarbonyl)-4-[(1-[[5-(dimethylamino)-1-naphthyl]sulfonyl]piperidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
IC50: above 0.013 mM
rel-(3S,3aR,6aS)-1-Acetyl-3-methyl-4-(2-oxo-3-phenylpropyl) hexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: 0.079 mM
rel-(3S,3aR,6aS)-1-Acetyl-3-methyl-4-(phenoxyacetyl)-hexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: 0.063 mM
rel-(3S,3aR,6aS)-1-Acetyl-3-methyl-4-[(1-methyl-1Hpyrrol-2-yl)(oxo)acetyl]hexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: 0.005 mM
rel-(3S,3aR,6aS)-1-Acetyl-3-methyl-4-[(2-phenylethyl)-sulfonyl]hexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: 0.045 mM
rel-(3S,3aR,6aS)-1-Acetyl-4-[2-(5-fluoro-2-methyl-1Hindol-3-yl)acetyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
-
IC50: 0.006 mM
trans-2-oxo-hexahydro-pyrrolo[3,2-b]pyrrolo-1,4-dicarboxylic acid 4-benzyl ester 1 tert butyl ester
-
0.5 mM, 6.3% inhibition after 15 min
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
compound binds to the dimer interface of the protease and disrupts dimerization
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
compound binds to the dimer interface of the protease and disrupts dimerization
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
compound binds to the dimer interface of the protease and disrupts dimerization
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
compound binds to the dimer interface of the protease and disrupts dimerization
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
compound binds to the dimer interface of the protease and disrupts dimerization
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
compound binds to the dimer interface of the protease and disrupts dimerization
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
compound binds to the dimer interface of the protease and disrupts dimerization
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
compound binds to the dimer interface of the protease and disrupts dimerization
additional information
-
the enzyme is inactivated by chemical crosslinking, indicating that the structural flexibility is essential for this enzyme
-
additional information
-
not inhibited by NaCl, CaCl2, EDTA, the enzyme does not contain enzymatically important cysteine residues or disulfide linkages
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycerol
-
promotes HCMV protease dimerization and subsequent proteolytic activity
additional information
-
self-interaction of pPR through its scaffolding domain plays an important role in activating the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009 - 0.033
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
0.092 - 0.097
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNASSRLA-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
-
dependent on enzyme concentration
0.0101 - 0.159
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
0.0042 - 0.0339
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2-'aminoethyl)-amino]naphthalenesulfonic acid
0.0118 - 0.0196
acetyl-Cys-tert-butylglycine-tert-butylglycine-Asn(Me)2-Ala-7-amido-4-methylcoumarin
-
24°C
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
-
0.009
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
-
-
0.033
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
-
-
0.0101
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, wild-typelike mutant enzyme A143Q
0.0145
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/H157E
0.0203
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/H157Q
0.0218
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/H157A
0.0277
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme S134A/A143Q
0.0356
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme S134A/A143Q/H157A
0.083
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.4, immobilized enzyme
0.159
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.4, enzyme in solution
0.0042
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2-'aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/R232H
0.0051
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2-'aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/D217N
0.0078
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2-'aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/D227N
0.0107
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2-'aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q
0.012
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2-'aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/L229R
0.0136
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2-'aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/S225Y/L229R
0.0339
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2-'aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/S225Y
0.125
Abz-GVVNASSRLAY(NO2)G
-
presence of 25% glycerol, enzyme HCMV A134Q
0.134
Abz-GVVNASSRLAY(NO2)G
-
presence of 50% glycerol, enzyme HCMV A134Q
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00833 - 0.0133
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
0.00061 - 0.046
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
0.000026 - 0.046
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
0.1 - 0.16
acetyl-Cys-tert-butylglycine-tert-butylglycine-Asn(Me)2-Ala-7-amido-4-methylcoumarin
-
24°C
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
0.00833
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
-
-
0.0133
4-(4'-dimethylaminophenazo)benzoic acid-RGVVNAS-2-aminobutanoyl-RLN-5-[(2'-aminoethyl)-amino]-naphthalene-1-sulfonic acid
-
-
0.00061
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme S134A/A143Q
0.00069
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme S134A/A143Q/H157A
0.0033
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/H157A
0.0036
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/H157Q
0.0041
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/H157E
0.033
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.2, 30°C, wild-typelike mutant enzyme A143Q
0.035
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.4, enzyme in solution
0.046
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-((2'-aminoethyl)amino)-naphthalene-1-sulfonic acid
-
pH 7.4, immobilized enzyme
0.000026
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/D227N
0.000027
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/L229R
0.000034
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/S225Y/L229R
0.00092
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/S225Y
0.0024
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/D217N
0.00348
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q/R232H
0.046
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
pH 7.2, 30°C, mutant enzyme A143Q
0.367
Abz-GVVNASSRLAY(NO2)G
-
presence of 50% glycerol, enzyme HCMV A134Q
0.583
Abz-GVVNASSRLAY(NO2)G
-
presence of 25% glycerol, enzyme HCMV A134Q
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
-
additional information
additional information
-
the turnover number for 4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala-(2'-aminoethyl)amino-naphthalene-1-sulfonic acid is less than 0.001/s, immobilized crosslinked enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00001
(2S)-2-[[(3aS,6S,6aR)-4-(1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000041
(2S)-2-[[(3aS,6S,6aR)-4-(4-chloro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000038
(2S)-2-[[(3aS,6S,6aR)-4-(4-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000027
(2S)-2-[[(3aS,6S,6aR)-4-(5-chloro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000022
(2S)-2-[[(3aS,6S,6aR)-4-(5-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000117
(2S)-2-[[(3aS,6S,6aR)-4-(5-methoxy[1,3]thiazolo[5,4-b]-pyridin-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.0000074
(2S)-2-[[(3aS,6S,6aR)-4-(6-ethylcarboxylate-1,2-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]-pyrrol-1(2H)yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000017
(2S)-2-[[(3aS,6S,6aR)-4-(6-fluoro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000043
(2S)-2-[[(3aS,6S,6aR)-4-(6-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000018
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-meth-yl5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropoxyphenyl)pyrrolidine-1-carboxamide
-
-
0.000038
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-chlorophenyl)pyrrolidine-1-carboxamide
-
-
0.000002
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000009
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-propoxyphenyl)pyrrolidine-1-carboxamide
-
-
0.000015
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-[4-(trifluoromethyl)phenyl]pyrrolidine-1-carboxamide
-
-
0.000016
(2S)-2-[[(3aS,6S,6aR)-4-[(-cis-2,3-dimethylcyclopropyl)-cis-carbonyl]-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.00001
(2S)-2-[[(3aS,6S,6aR)-4-[5-[(difluoromethyl)sulfonyl]-1,3-benzothiazol-2-yl]-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)-pyrrolidine-1-carboxamide
-
-
0.00004
(2S)-2-[[(3aS,6S,6aR)-4-[6-(hydroxymethyl)-1,3-benzothiazol-2-yl]-6-methyl-5-oxohexahydropyrrolo[3,2-b]-pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000025
(2S)-2-[[(3aS,6S,6aR)-6-methyl-4-(6-nitro-1,3-benzothiazol-2-yl)-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000446
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-(1,3-thiazol-2-yl)hexahydropyrrolo[3,2-b]pyrrol-1(2H)yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.000021
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-[1,3]thiazolo-[5,4-b]pyridin-2-ylhexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.00002
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-[6-(trifluoromethoxy)-1,3-benzothiazol-2-yl]hexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
-
-
0.00004
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-(2-naphthylsulfonyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.00006
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-(1-naphthylsulfonyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.000079
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-(4-propoxybenzoyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.000033
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-[(4-propoxyphenyl)sulfonyl]pyrrolidin-2-yl]-carbonyl]hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.00002
(3S,3aR,6aS)-1-(Cyclopropylcarbonyl)-4-[((2S)-1-[[5-(dimethylamino)-1-naphthyl]sulfonyl]pyrrolidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
-
-
0.000039
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[(4-isopropoxyphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.000099
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[(4-isopropylphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.00002
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[[5-(dimethylamino)-1-naphthyl]sulfonyl]pyrrolidin-2-yl]-carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.000034
(3S,3aR,6aS)-1-Acetyl-4-[((2S)-1-[[5-(dimethylamino)-1-naphthyl] sulfonyl]pyrrolidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.000021
(3S,3aR,6aS)-4-[[(2S)-1-(1,1'-biphenyl-4-ylcarbonyl)-pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
-
-
0.000002
(3S,3aR,6aS)-4-[[(2S)-1-[(5-chloro-3-methyl-1-benzothien-2-yl)carbonyl]pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2]pyrrol-2(1H)-one
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00018
(2S)-2-[[(3aS,6S,6aR)-4-(1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00018 mM
0.00029
(2S)-2-[[(3aS,6S,6aR)-4-(4-chloro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00029 mM
0.00024
(2S)-2-[[(3aS,6S,6aR)-4-(4-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00024 mM
0.0011
(2S)-2-[[(3aS,6S,6aR)-4-(4-methoxy-7-methyl-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]-pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.0011 mM
0.00046
(2S)-2-[[(3aS,6S,6aR)-4-(5-chloro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00046 mM
0.00023
(2S)-2-[[(3aS,6S,6aR)-4-(5-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00023 mM
0.00087
(2S)-2-[[(3aS,6S,6aR)-4-(5-methoxy[1,3]thiazolo[5,4-b]-pyridin-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00087 mM
0.00035
(2S)-2-[[(3aS,6S,6aR)-4-(6-ethylcarboxylate-1,2-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]-pyrrol-1(2H)yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00035 mM
0.00036
(2S)-2-[[(3aS,6S,6aR)-4-(6-fluoro-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00036 mM
0.00022
(2S)-2-[[(3aS,6S,6aR)-4-(6-methoxy-1,3-benzothiazol-2-yl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00022 mM
0.00018
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-meth-yl5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropoxyphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00018 mM
0.00065
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(1-naphthyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00065 mM
0.0014
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(3-chlorophenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.0014 mM
0.00026
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-chlorophenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00026 mM
0.0002
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.0002 mM
0.00021
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-propoxyphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00021 mM
0.00023
(2S)-2-[[(3aS,6S,6aR)-4-(cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-[4-(trifluoromethyl)phenyl]pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00023 mM
0.0003
(2S)-2-[[(3aS,6S,6aR)-4-[(-cis-2,3-dimethylcyclopropyl)-cis-carbony]-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.0003 mM
0.0018
(2S)-2-[[(3aS,6S,6aR)-4-[(-cis-2,3-dimethylcyclopropyl)-trans-carbonyl]-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.0018 mM
0.00021
(2S)-2-[[(3aS,6S,6aR)-4-[5-[(difluoromethyl)sulfonyl]-1,3-benzothiazol-2-yl]-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)-pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00021 mM
0.00031
(2S)-2-[[(3aS,6S,6aR)-4-[6-(hydroxymethyl)-1,3-benzothiazol-2-yl]-6-methyl-5-oxohexahydropyrrolo[3,2-b]-pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00031 mM
0.0087
(2S)-2-[[(3aS,6S,6aR)-6-methyl-4-(4-nitrophenyl)-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.0087 mM
0.00039
(2S)-2-[[(3aS,6S,6aR)-6-methyl-4-(6-nitro-1,3-benzothiazol-2-yl)-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00039 mM
0.0015
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-(1,3-thiazol-2-yl)hexahydropyrrolo[3,2-b]pyrrol-1(2H)yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.0015 mM
0.02
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-[(2,2,3,3-tetramethylcyclopropyl)carbonyl]hexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: above 0.02 mM
0.00029
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-[1,3]thiazolo-[5,4-b]pyridin-2-ylhexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00029 mM
0.00046
(2S)-2-[[(3aS,6S,6aR)-6-methyl-5-oxo-4-[6-(trifluoromethoxy)-1,3-benzothiazol-2-yl]hexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]-N-(4-isopropylphenyl)pyrrolidine-1-carboxamide
Human betaherpesvirus 5
-
IC50: 0.00046 mM
1
(3aR,6R,6aS)-4-Acetyl-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 1 mM
0.006
(3aS,6S,6aR)-4-(2-Etoxy-acetyl)-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.006 mM
0.11 - 0.79
(3aS,6S,6aR)-4-Acetyl-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
0.159
(3R,3aS,6aR)-1-Acetyl-3-methyl-4-([(2S)-1-[(4-methylphenyl) sulfonyl]pyrrolidin-2-yl]carbonyl)hexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.159 mM
0.5
(3R,3aS,6aR)-1-Acetyl-4-[((2S)-1-[[5-(dimethylamino)-1-naphthyl] sulfonyl]pyrrolidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.5
(3R,3aS,6aR)-1-Acetyl-4-[[(2S)-1-benzoylpyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.00019
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-(2-naphthylsulfonyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: below 0.00019 mM
0.00037
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-(1-naphthylsulfonyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.00037 mM
0.00054
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-(4-propoxybenzoyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.00054 mM
0.00023
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)-1-[(4-propoxyphenyl)sulfonyl]pyrrolidin-2-yl]-carbonyl]hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.00023 mM
0.0018
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-3-methyl-4-[[(2S)1-(phenylsulfonyl)pyrrolidin-2-yl]carbonyl]-hexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.0018 mM
0.065
(3S,3aR,6aS)-1-(Cyclopropylcarbonyl)-4-([(2S)-1-[(3-isopropoxyphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.065 mM
0.00034
(3S,3aR,6aS)-1-(Cyclopropylcarbonyl)-4-[((2S)-1-[[5-(dimethylamino)-1-naphthyl]sulfonyl]pyrrolidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.00034 mM
0.00039
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-(4-isopropylbenzoyl)pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)
Human betaherpesvirus 5
-
IC50: 0.00039 mM
0.065
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[(3-isopropoxyphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.065 mM
0.0004
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[(4-isopropoxyphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.0004 mM
0.00046
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[(4-isopropylphenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.00046 mM
0.00034
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[[5-(dimethylamino)-1-naphthyl]sulfonyl]pyrrolidin-2-yl]-carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.00034 mM
0.0011
(3S,3aR,6aS)-1-(cyclopropylcarbonyl)-4-[[(2S)-1-[[6-(dimethylamino)-1-naphthyl]sulfonyl]pyrrolidin-2-yl]-carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.0011 mM
0.014
(3S,3aR,6aS)-1-Acetyl-3-methyl-4-([(2S)-1-[(4-methylphenyl) sulfonyl]pyrrolidin-2-yl]carbonyl)hexahydropyrrolo-[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.014 mM
0.00054
(3S,3aR,6aS)-1-Acetyl-4-[((2S)-1-[[5-(dimethylamino)-1-naphthyl] sulfonyl]pyrrolidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.00054 mM
0.05
(3S,3aR,6aS)-1-Acetyl-4-[[(2S)-1-benzoylpyrrolidin-2-yl]carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.05 mM
0.0003
(3S,3aR,6aS)-4-[[(2S)-1-(1,1'-biphenyl-4-ylcarbonyl)-pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.0003 mM
0.0014
(3S,3aR,6aS)-4-[[(2S)-1-(4-chlorobenzoyl)pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-1(2H)-one
Human betaherpesvirus 5
-
IC50: 0.0014 mM
0.0021
(3S,3aR,6aS)-4-[[(2S)-1-(benzylsulfonyl)pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.0021 mM
0.00084
(3S,3aR,6aS)-4-[[(2S)-1-[(4-chlorophenyl)sulfonyl]pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.00084 mM
0.00019
(3S,3aR,6aS)-4-[[(2S)-1-[(5-chloro-3-methyl-1-benzothien-2-yl)carbonyl]pyrrolidin-2-yl]carbonyl]-1-(cyclopropylcarbonyl)-3-methylhexahydropyrrolo[3,2]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: 0.00019 mM
0.00014
3-[((2S)-2-[[(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]carbonyl]pyrrolidin-1-yl)sulfonyl]-N,N-dimethylbenzamide
Human betaherpesvirus 5
-
IC50: 0.00014 mM
0.0022
3-[[((2S)-2-[[(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-carbonyl]pyrrolidin-1-yl)sulfonyl]methyl]-N,N-dimethylbenzamide
Human betaherpesvirus 5
-
IC50: 0.0022 mM
0.013
4-(2-Etoxy-acetyl)-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.013 mM
0.007
N-[(1S)-2-[rel-(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-1-methyl-2-oxoethyl]-5-(dimethylamino)naphthalene-1-sulfonamide
Human betaherpesvirus 5
-
IC50: 0.007 mM
0.001 - 0.367
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
0.0037 - 0.094
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
0.1
N-[2-[rel-(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrol-1(2H)-yl]-2-oxoethyl]-5-(dimethylamino)-N-methylnaphthalene-1-sulfonamide
Human betaherpesvirus 5
-
IC50: above 0.1 mM
0.805
rel-(3aS,6R,6aR)-4-acetoxyacetyl-6-methyl-5-oxohexahydro-pyrrolo[3,2-b]pyrrolo-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.805 mM
1.8
rel-(3aS,6R,6aR)-4-acetyl-6-methyl-5-oxo-hexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 1.8 mM, 0.5 mM, 15.4% inhibition after 15 min
0.5
rel-(3aS,6S,6aR)-4-(2,2-Dimethylpropanoyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.5
rel-(3aS,6S,6aR)-4-(2,4-Dinitrophenyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.5
rel-(3aS,6S,6aR)-4-(2-Hydroxy-3-phenoxypropyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.133
rel-(3aS,6S,6aR)-4-(3-Hydroxypropanoyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.133 mM
0.5
rel-(3aS,6S,6aR)-4-(4-Methoxybenzoyl)-6-methyl-5-oxohexahydropyrrolo [3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.0115
rel-(3aS,6S,6aR)-4-(Bicyclo[4.2.0]octa-1,3,5-trien-7-ylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.0115 mM
0.072
rel-(3aS,6S,6aR)-4-(cis-2,3-Dimethylcyclopropanecarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.072 mM
0.032
rel-(3aS,6S,6aR)-4-(cyclobutylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.032 mM
0.009
rel-(3aS,6S,6aR)-4-(Cyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.009 mM
0.5
rel-(3aS,6S,6aR)-4-(Dimethoxyphosphoryl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.5
rel-(3aS,6S,6aR)-4-(Hydroxymethyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.1
rel-(3aS,6S,6aR)-4-(trans-2,3-Dimethylcyclopropylcarbonyl)-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.1 mM
0.398
rel-(3aS,6S,6aR)-4-Formyl-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.398 mM
0.126
rel-(3aS,6S,6aR)-4-Isobutyryl-6-methyl-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.126 mM
0.5
rel-(3aS,6S,6aR)-6-Methyl-4-(methylthio)-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.01
rel-(3aS,6S,6aR)-6-Methyl-4-[(2-methylcyclopropyl)-carbonyl]-5-oxohexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.01 mM
0.25
rel-(3aS,6S,6aR)-6-Methyl-5-oxo-4-(1H-pyrrol-1-ylcarbonyl)-hexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.25 mM
0.5
rel-(3aS,6S,6aR)-6-Methyl-5-oxo-4-(2,2,3,3-tetramethylcyclopropylcarbonyl) hexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.5
rel-(3aS,6S,6aR)-6-Methyl-5-oxo-4-[(1E)-3-oxobut-1-enyl]-hexahydropyrrolo[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: above 0.5 mM
0.013
rel-(3S,3aR,6aS)-1-(Cyclopropylcarbonyl)-4-[(1-[[5-(dimethylamino)-1-naphthyl]sulfonyl]piperidin-2-yl)carbonyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2(1H)-one
Human betaherpesvirus 5
-
IC50: above 0.013 mM
0.079
rel-(3S,3aR,6aS)-1-Acetyl-3-methyl-4-(2-oxo-3-phenylpropyl) hexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.079 mM
0.063
rel-(3S,3aR,6aS)-1-Acetyl-3-methyl-4-(phenoxyacetyl)-hexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.063 mM
0.005
rel-(3S,3aR,6aS)-1-Acetyl-3-methyl-4-[(1-methyl-1Hpyrrol-2-yl)(oxo)acetyl]hexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.005 mM
0.045
rel-(3S,3aR,6aS)-1-Acetyl-3-methyl-4-[(2-phenylethyl)-sulfonyl]hexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.045 mM
0.006
rel-(3S,3aR,6aS)-1-Acetyl-4-[2-(5-fluoro-2-methyl-1Hindol-3-yl)acetyl]-3-methylhexahydropyrrolo[3,2-b]pyrrol-2-one
Human betaherpesvirus 5
-
IC50: 0.006 mM
0.11
(3aS,6S,6aR)-4-Acetyl-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.11 mM
0.79
(3aS,6S,6aR)-4-Acetyl-6-methyl-5-oxohexahydropyrrolo-[3,2-b]pyrrole-1-carboxylic acid benzyl ester
Human betaherpesvirus 5
-
IC50: 0.79 mM
0.001
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
Human gammaherpesvirus 8
-
pH 8.0, temperature not specified in the publication
0.004
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
Human gammaherpesvirus 4
-
pH 8.0, temperature not specified in the publication
0.0047
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
Human betaherpesvirus 5
-
pH 8.0, temperature not specified in the publication
0.367
N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
Human alphaherpesvirus 2
-
pH 8.0, temperature not specified in the publication
0.0037
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
Human gammaherpesvirus 8
-
pH 8.0, temperature not specified in the publication
0.019
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
Human gammaherpesvirus 4
-
pH 8.0, temperature not specified in the publication
0.0388
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
Human betaherpesvirus 5
-
pH 8.0, temperature not specified in the publication
0.094
N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
Human alphaherpesvirus 2
-
pH 8.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
95586, 95591, 95592, 95593, 95594, 95596, 95597, 95598, 95600, 95601, 95602, 95603, 95604, 95605, 95607, 95608, 95609, 95610, 95611, 649131, 650071, 650227, 650245, 652724, 652734, 652751, 653074, 653320, 653855, 663617, 666188, 677592, 681048, 681686, 731318, 732540
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
bioinformatic analyses identify SFA homologs in three subgroups of the alveolates, namely the apicomplexans, ciliates, and dinoflagellates, as well as in two subgroups of the stramenopiles, namely the diatoms and oomycetes
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
using immunofluorescence assays staining of the two basal bodies and an anteriorly directed striated fiber in the flagellar apparatus of biflagellate Phytophthora zoospores is obtained
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Herpes simplex virus
-
in a protease deletion mutant, capsids are assembled and portal protein is incorporated into capsids. Mutant does not replicate to appreciable extents on CV1 cells. The presence of the viral protease is required for immunoreactivity at the capsid surface with portal specific antibody
Show AA Sequence and Transmembrane Helices (1132 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
-
2 * 27000, I-site mutant A134V, sedimentation equilibrium centrifugation of diluted enzyme solution
29700
-
sedimentation equilibrium centrifugation in absence of glycerol
48500
-
sedimentation equilibrium centrifugation in presence of 20% glycerol
54000 - 56000
-
I-site mutant A143V, sedimentation equilibrium centrifugation, the value is concentration-dependent
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
-
the active two-chain assemblin can be formed from the independently cloned and expressed subunits An and Ac
dimer
-
the catalytically active dimer is significantly dissociated above 25°C
dimer
-
2 * 27000, I-site mutant A134V, sedimentation equilibrium centrifugation of diluted enzyme solution
dimer
-
dimeric form is necessary to activate the enzyme because of an induced stabilization of the oxyanion hole
dimer
-
dimerization is required for catalytic activity, appropriate dimer formation may be required to indirectly stabilize the protease oxyanion hole revealing a novel mechanism for dimerization to regulate enzyme activity
dimer
-
the enzyme exists in a monomer/dimer equilibrium in solution, but only the dimer form is catalytically active. The stability of the dimer is affected by the presence of anti-chaotrophic agents
additional information
concentration-dependent equilibrium of monomeric and dimeric protease in solution, small-angle X-ray scattering
additional information
-
concentration-dependent equilibrium of monomeric and dimeric protease in solution, small-angle X-ray scattering
additional information
Suid alphaherpesvirus 1 Kaplan
-
concentration-dependent equilibrium of monomeric and dimeric protease in solution, small-angle X-ray scattering
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
expressed in virus-infected cells as a 709-residue precursor that undergoes two autocatalytic cleavages to generate the mature enzyme form
proteolytic modification
-
the proteinase is synthesized as an enzymatiacally active precursor that undergoes several autoproteolytic cleavages. Two of these are common in all herpes group viruses, one occurs toward the carboxyl end of the precursor, i.e. M-site, and the other near the middle at the R-site. The R-site cleavage divides the precusor into assemblin and a nonproteolytic carboxyl half. CMV proteinase undergoes a third autoproteolytic cleavage that divides assemblin into approximately equal-size An and Ac subunits. None of these cleavages is absolutely necessary for enzyme activity
proteolytic modification
-
the enzyme is cleaved as an enzymatically active 74000 Da precursor that cleaves itself at four sites
proteolytic modification
-
the enzyme contains an internal (I) cleavage site. Blocking this site for cleavage in I- mutant virus shows increased amounts of a fragment produced by cleavage at the nearby cryptic site, suggesting that its replication may bypass the I-site block by using the C site as an alternative cleavage pathway. I-site cleavage destabilizes assemblin and its fragments, whereas C-site cleavage does not
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of HAS-2 with covalently bound diisopropyl fluorophosphate
Herpes simplex virus
-
in complex with inhibitors {N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide and N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
-
crystal structure of HCMV protease in complex with the peptidomimetic inhibitor BILC 821 as protease model. Only the dimeric form of the protease is able to reorient the main-chain atoms of Arg165 along the reaction coordinate in order to stabilize more efficiently the oxyanion formed in the reaction pathway
-
hanging drop method, microseeding technique, each of six components in the final crystallization formula (16% polyethylene glycol 4000, 0.1 M MES pH 6.0, 0.4 M LiCl, 10% glycerol 5% tert-butanol and 5 mM Na2S2O3) plays a distinctive role and is indispensable. Free enzyme crystallizes at pH 6.0. Using 20-50 mM spermine in the crystallization buffer, crystals of two peptidomimetic inhibitor complexes with C821 are obtained at pH 7.5 and pH 8.0. Spermine is required for the inhibitor complexes to be crystallized at pH 8.0, possibly neutralizing net negative charges of the enzyme owing to its acidic pI of 5.5
-
hanging-drop vapor diffusion method, crystal structure of the wild-typelike mutant enzyme A143Q in complex with peptidomimetic inhibitors, crystal structure of peptidomimetic inhibitor in complex with the E31R mutant enzyme
-
sitting-drop vapour diffusion method, crystals of the S225Y mutant in complex with the peptidomimetic inhibitor BILC408
-
in complex with inhibitors 3_4_21-97_3-cp2 and 3_4_21-97_3-cp3
structures of native monomeric, active dimeric, and diisopropyl fluorophosphate-inhibited dimeric protease, to respective resolutions of 2.05, 2.10 and 2.03 A. In the dimeric form, a functional oxyanion hole is formed by a loop of 10 aminoacid residues encompassing two consecutive arginine residues (Arg136 and Arg137). In the monomeric form, the top of the loop is shifted by approximately 11 A, resulting in a complete disruption of the oxyanion hole and loss of activity. The dimerization-induced allosteric changes are basis for the concentration-dependent activation of the protease
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H61A
Herpes simplex virus
-
mutation impairs protease activity. Morphology of mutant capsids exclusively resembles those of procapsids or large cored B capsids. Specifically, mutant capsids are spherical and lack electron dense cores. Most of these particles are tightly clustered in the nucleoplasm. Mutant does not replicate to appreciable extents on CV1 cells
A143Q
-
all enzyme samples used in this experiments contain an additional mutation, A143Q. The mutation disables one of the internal cleavage sites but has little effects on the kinetic properties of the enzyme
A143Q/D217N
-
the ratio of turnover number to Km-value is 11% of that for mutant enzyme A143Q
A143Q/D227N
-
the ratio of turnover number to Km-value is 1273fold lower than that for mutant A143Q
A143Q/E31R
-
the ratio of turnover number to Km-value is 44.6fold lower than that for the wild-typelike mutant A143Q
A143Q/E31S
-
the ratio of turnover number to Km-value is 4.8fold lower than that for the wild-typelike mutant A143Q
A143Q/H157A
-
the ratio of turnover number to Km-value is 22fold lower than that of the wild-typelike mutant enzyme A143Q
A143Q/H157E
-
the ratio of turnover number to Km-value is 11.7fold lower than that of the wild-typelike mutant enzyme A143Q
A143Q/H157Q
-
the ratio of turnover number to Km-value is 19fold lower than that of the wild-typelike mutant enzyme A143Q
A143Q/L229R
A143Q/R137E
-
the ratio of turnover number to Km-value is 6.3fold lower than that for the wild-typelike mutant A143Q
A143Q/R232H
-
mutant enzyme A143Q/R232H essentially maintains wild-type catalytic activity, shows little change in the CD spectra compared to mutant A143Q enzyme, thermal stability is similar to that of mutant A143Q enzyme. The ratio of turnover number to Km-value is 5.1fold lower than that for mutant enzyme A143Q
A143Q/S225Y
-
mutant enzyme with large conformational changes with 40% lower helical content relative to the mutant enzyme A143Q, mutant dimer has similar stability to the mutant A143Q dimer. Many of the conformational differences between the mutant A143Q and the mutant enzyme A143Q/S225Y are likely the direct result of the mutation itself. alphaF helix tilts away from the wild type dimer two-fold axis in the S225Y mutant, creating a space near the two-fold axis to accomodate the new Tyr side chain. The S225Y mutation is the likely trigger for the change in the monomer conformation and the dimer organization, significant lower thermal stability than the mutant enzyme A143Q. The ratio of turnover number to Km-value is 1273fold lower than that for mutant enzyme A143Q
A143Q/S225Y/L229R
-
mutation has little effect on the stability of the dimer, mutant enzyme with large conformational changes with 40% lower helical content relative to the mutant enzyme A143Q, significant lower thermal stability than the mutant enzyme A143Q. The ratio of turnover number to Km-value is 1680fold lower than that for mutant enzyme A143Q
A143T/A144T
-
mutant displays better stability than wild-type and has esterase activity toward specific small ester compounds, e.g., Boc-L-Ala-4-nitrophenol
A143V
-
inability of the mutant virus to effect I-site cleavage in infected cells, mutation has no gross effect on the rate of virus production or on the amounts of extracellular virions, noninfectious enveloped particles and dense bodies
H47A
-
inactive mutant, active if coexpressed with AW5 which encodes the first 179 amino acids of assemblin with the addition of Ile, Gln, Thr
S118A
-
inactive mutant, active if coexpressed with AW5 which encodes the first 179 amino acids of assemblin with the addition of Ile, Gln, Thr
S132A
S134A/A143Q
-
the ratio of turnover number to Km-value is 150fold lower than that of the wild-typelike mutant enzyme A143Q
S134A/A143Q/H157A
-
the ratio of turnover number to Km-value is 174fold lower than that of the wild-typelike mutant enzyme A143Q
V141G/V207G
-
soluble and stable, indistinguishable from wild-type in vitro
H47A
-
mutation prevents I-site cleavage (cleavage at an internal site of assemblin, converting it to a two-chain form that remain active). Imidazole restores I-site cleavage to mutant
additional information
A143Q/L229R
-
mutant enzyme A143Q/L229R shows approximately a 20% decrease in helical content relative to the mutant enzyme A143Q, mutant enzyme A143Q/L229R has significant lower thermal stability than the mutant enzyme A143Q
A143Q/L229R
-
mutation has little effect on the stability of the dimer, significant lower thermal stability than the mutant enzyme A143Q. The ratio of turnover number to Km-value is 1826fold lower than that for mutant enzyme A143Q
additional information
-
stabilized against self-cleavage by a single point mutation in its cleavage site (IC-assemblin)
additional information
-
IC-assemblin and IC-assemblinHis mutants of assemblin, blocked for internal and cryptic site cleavage. Enzymatic activities of pPR mutants are indistinguishable from that of IC-assemblin
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
10 min 50% loss of activity of mutant enzyme A143Q/D227N and A143Q/S225Y/L229R
35
-
10 min, 50% loss of activity of mutant enzymes A143Q and A143Q/R232H
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dimers of the enzyme are stabilized in high-salt buffer. The Kd for the dimer decreases by 260fold, from 0.008 mM to 31 nM, going from the low-salt to the high-salt buffer
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM HEPES, 0.1 mM EDTA, 1 mM DTT, 100 mM NaCl, 50% glycerol, pH 7.5, protein concentration 0.12 mg/ml, stable 8 months or longer
-
-70°C, 50 mM Tris-HCl, pH 8.0, 100 mM NaCl, 1 mM DTT, 1 mM EDTA, 20% glycerol, stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of HCMV protease with N-(5'-phosphoribosyl)anthranilate isomerase substrate in Saccharomyces cerevisiae RLY07 strain. HCMV protease expressed from the full-length GAL1 promoter, subcloned on a GAL1 vector series, with discrete protein production levels of 71%, 46%, and 16% compared to the original 100% promoter
-
expressed in Escherichia coli
into the NdeI and HindIII sites of pET-17b vector and expressed in Escherichia coli BL21(DE3)pLysS
-
separate cloning of the two chains An and Ac, expression in Sf9 cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
cell growth selection system in the yeast Saccharomyces cerevisiae that can detect and characterize HCMV protease activity and is applicable to screen for HCMV protease inhibitors in a high-throughput format
medicine
-
targeting prodrugs for activation by a specific protease encoded by the infectious HCMV pathogen may be achievable. Dipeptide prodrug of ganciclovir, acetyl-L-Gln-L-Ala-ganciclover, is a potential selective prodrug candidate
additional information
-
conformational changes of the dimer upon covalent binding reproduced by molecular dynamics simulations of the noncovalent complex model, demonstrating that the HCMV protease operates by an induced-fit mechanism. Catalytic activity of the dimer is a result of more favorable interactions between the oxyanion in the covalently bound state and the backbone nitrogen of Arg165
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kan, C.C.
Cytomegalovirus assemblin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
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Human betaherpesvirus 5, simian cytomegalovirus
-
brenda
Darke, P.L.
Herpesvirus assemblin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
470-472
1998
Bovine alphaherpesvirus 1, Equid alphaherpesvirus 1, equine herpesvirus type 2, Herpes simplex virus, Human alphaherpesvirus 1, Human alphaherpesvirus 2, Saimiriine gammaherpesvirus 2, Suid alphaherpesvirus 1
-
brenda
Jupp, R.; Mills, J.; Tigue, N.J.; Kay, J.
Human herpesvirus type 6 assemblin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
472-474
1998
Human betaherpesvirus 6
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brenda
Jupp, R.; Ritchie, A.; Robinson, M.; Broadhurst, A.; Mills, J.
Epstein-Barr virus assemblin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
474-476
1998
Human gammaherpesvirus 4
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brenda
McMillan, D.M.; Jupp, R.; Mills, J.; Kay, J.
Varicella-zoster virus assemblin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
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Human alphaherpesvirus 3
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brenda
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Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad
Cell
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Human betaherpesvirus 5
brenda
Holwerda, B.
Activity in monomers of human cytomegalovirus protease
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259
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Human betaherpesvirus 5
brenda
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beta-Lactam derivatives as inhibitors of human cytomegalovirus protease
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41
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Human betaherpesvirus 5
brenda
Tomasselli, A.G.; Paddock, D.J.; Curry, K.A.; Garlick, R.L.; Leone, J.W.; Lull, J.M.; Mutchler, V.T.; Baker, C.A.; Cavey, G.S.; Methews, W.R.; Shelly, J.A.; Finzel, B.C.; Baldwin, E.T.; Wells, P.A.; Tomich, C.S.C.
Recombinant human cytomegalovirus protease with a C-terminal (His)6 extension: purification, autocatalytic release of the mature enzyme, and biochemical characterization
Protein Expr. Purif.
14
343-352
1996
Human betaherpesvirus 5
brenda
McKercher, G.; Bonneau, P.R.; Lagace, L.; Thibeault, D.; Massaiol, M.J.; Krogsrud, R.; Lawetz, C.; McDonald, P.C.; Cordingley, M.G.
Improved purification protocol of the HSV-1 protease catalytic domain, using immunoaffinity
Biochem. Cell Biol.
75
795-801
1997
Human alphaherpesvirus 1
brenda
Gibson, W.; Hall, M.R.T.
Assemblin, an essential herpesvirus proteinase
Drug Des. Discov.
15
39-47
1997
Human betaherpesvirus 5
brenda
Hall, M.R.T.; Gibson, W.
Independently cloned halves of cytomegalovirus assemblin An and Ac can restore proteolytic activity to assemblin mutants by intermolecular complementation
J. Virol.
71
956-964
1997
Human betaherpesvirus 5
brenda
Bonneau, P.R.; Grand-Maitre, C.; Greenwood, D.J.; Lagac, L.; LaPlante, S.R.; Massariol., M.J.; Ogilvie, W.W.; OMeara, J.A.; Kawai, S.H.
Evidence of a conformational change in the human cytomegalovirus protease upon binding of peptidyl-activated carbonyl inhibitors
Biochemistry
36
12644-12652
1997
Human betaherpesvirus 5
brenda
Hoog, S.S.; Smith, W.W.; Qiu, X.; Janson, C.A.; Hellmig, B.; McQuerney, M.S.; ODonnell, K.; OShannessy, D.; DiLella, A.G.; Abdel-Meguid, S.S.
Active site cavity of herpesvirus protease revealed by the crystal structure of Herpes simplex virus protease/inhibitor complex
Biochemistry
36
14023-14029
1997
Herpes simplex virus, Human alphaherpesvirus 1
brenda
Margosiak, S.A.; Vanderpool, D.L.; Sisson, W.; Pinko, C.; Kan, C.C.
Dimerization of the human cytomegaolvirus protease: kinetic and biochemical characterization of the catalytic homodimer
Biochemistry
35
5300-5307
1996
Human betaherpesvirus 5
brenda
Shieh, H.S.; Kurumbail, R.G.; Stevens, A.M.; Stegeman, R.A.; Sturman, E.J.; Pak, J.Y.; Wittwer, A.J.; Palmier, M.O.; Wiegand, R.C.; Holwerda, B.C.; Stallings, W.C.
Three-dimensional structure of human cytomegalovirus protease
Nature
383
279-282
1996
Human betaherpesvirus 5
brenda
Tong, L.; Qian, C.; Massariol, M.J.; Bonneau, P.R.; Cordingley, M.G.; Lagace, L.
A new serine-protease fold revealed by the crystal strucutre of human cytomegalovirus protease
Nature
383
272-275
1996
Human betaherpesvirus 5
brenda
Snyder, S.W.; Edalji, R.P.; Lindh, F.G.; Walter, K.A.; Solomon, L.; Pratt, S.; Steffy, K.; Holzman, T.F.
Initial characterization of autoprocessing and active-center mutants of CMV proteinase
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15
763-774
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Human betaherpesvirus 5
brenda
LaFemina, R.L.; Bakshl, K.; Long, W.J.; Pramanik, B.; Veloski, C.A.; Wolanski, B.S.; Marcy, A.L.; Hazuda, D.J.
Characterization of a soluble stable human cytomegalovirus protease and inhibition by M-site peptide mimics
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70
4819-4824
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Human betaherpesvirus 5
brenda
Darke, P.L.; Cole, J.L.; Waxman, L.; Hall, D.L.; Sardana, K.; Kuo, L.C.
Active human cytomegalovirus protease is a dimer
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271
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Human betaherpesvirus 5
brenda
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Purification of active Herpes simplex virus-1 protease expressed in Escherichia coli
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Human alphaherpesvirus 1
brenda
Hall, M.R.T.; Gibson, W.
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brenda
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Purification and kinetic characterization of human cytomegalovirus assemblin
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Human betaherpesvirus 5
-
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Human betaherpesvirus 5, Human betaherpesvirus 6
brenda
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69
1265-1270
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Human gammaherpesvirus 4, Human betaherpesvirus 5
brenda
McMillan, D.J.; Kay, J.; Mills, J.S.
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78
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Human alphaherpesvirus 3
brenda
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A rational approach towards successful crystallization and crystal treatment of human cytomegalovirus protease and its inhibitor complex
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56
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Human betaherpesvirus 5
brenda
Khayat, R.; Batra, R.; Massariol, M.J.; Lagace, L.; Tong, L.
Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease
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40
6344-6351
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Human betaherpesvirus 5
brenda
Khayat, R.; Batra, R.; Qian, C.; Halmos, T.; Bailey, M.; Tong, L.
Structural and biochemical studies of inhibitor binding to human cytomegalovirus protease
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Human betaherpesvirus 5
brenda
Khayat, R.; Batra, R.; Bebernitz, G.A.; Olson, M.W.; Tong, L.
Characterization of the monomer-dimer equilibrium of human cytomegalovirus protease by kinetic methods
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43
316-322
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Human betaherpesvirus 5
brenda
Borthwick, A.D.; Angier, S.J.; Crame, A.J.; Exall, A.M.; Haley, T.M.; Hart, G.J.; Mason, A.M.; Pennell, A.M.; Weingarten, G.G.
Design and synthesis of pyrrolidine-5,5-trans-lactams (5-oxo-hexahydro-pyrrolo[3,2-b]pyrroles) as novel mechanism-based inhibitors of human cytomegalovirus protease. 1. The alpha-methyl-trans-lactam template
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43
4452-4464
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Human betaherpesvirus 5
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45
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Human betaherpesvirus 5
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Design and synthesis of pyrrolidine-5,5'-trans-lactams (5-oxo-hexahydropyrrolo[3,2-b]pyrroles) as novel mechanism-based inhibitors of human cytomegalovirus protease. 4. Antiviral activity and plasma stability
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46
4428-4449
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Human betaherpesvirus 5
brenda
Chan, C.K.; Brignole, E.J.; Gibson, W.
Cytomegalovirus assemblin (pUL80a): cleavage at internal site not essential for virus growth; proteinase absent from virions
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76
8667-8674
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Human betaherpesvirus 5
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8
810-817
2001
Human betaherpesvirus 5
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de Oliveira, C.A.; Guimaraes, C.R.; Barreiro, G.; de Alencastro, R.B.
Investigation of the induced-fit mechanism and catalytic activity of the human cytomegalovirus protease homodimer via molecular dynamics simulations
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52
483-491
2003
Human betaherpesvirus 5
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geitmann, M.; Danielson, E.H.
Studies of substrate-induced conformational changes in human cytomegalovirus protease using optical biosensor technology
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Human betaherpesvirus 5
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Chemical rescue of I-site cleavage in living cells and in vitro discriminates between the cytomegalovirus protease, assemblin, and its precursor, pUL80a
J. Biol. Chem.
280
33206-33212
2005
simian cytomegalovirus
brenda
Loveland, A.N.; Chan, C.K.; Brignole, E.J.; Gibson, W.
Cleavage of human cytomegalovirus protease pUL80a at internal and cryptic sites is not essential but enhances infectivity
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79
12961-12968
2005
Human betaherpesvirus 5
brenda
Cottier, V.; Barberis, A.; Luethi, U.
Novel yeast cell-based assay to screen for inhibitors of human cytomegalovirus protease in a high-throughput format
Antimicrob. Agents Chemother.
50
565-571
2006
Human betaherpesvirus 5
brenda
Fernandes de Oliveira, C.A.; Werneck Guimaraes, C.R.; Barreiro, G.; Bicca de Alencastro, R.
Human cytomegalovirus protease: Why is the dimer required for catalytic activity?
J. Chem. Theory Comput.
3
278-288
2007
Human betaherpesvirus 5
brenda
Brignole, E.J.; Gibson, W.
Enzymatic activities of human cytomegalovirus maturational protease assemblin and its precursor (pPR, pUL80a) are comparable: [corrected] maximal activity of pPR requires self-interaction through its scaffolding domain
J. Virol.
81
4091-4103
2007
Human betaherpesvirus 5
brenda
Harper, J.D.; Thuet, J.; Lechtreck, K.F.; Hardham, A.R.
Proteins related to green algal striated fiber assemblin are present in stramenopiles and alveolates
Protoplasma
236
97-101
2009
Paramecium tetraurelia, Perkinsus marinus, Phaeodactylum tricornutum, Phytophthora infestans, Phytophthora nicotianae, Phytophthora ramorum, Phytophthora sojae, Tetrahymena thermophila, Thalassiosira pseudonana
brenda
Fernandes, S.; Brignole, E.; Taori, K.; Gibson, W.
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85
3526-3534
2011
Cytomegalovirus
brenda
Gable, J.; Lee, G.; Jaishankar, P.; Hearn, B.; Waddling, C.; Renslo, A.; Craik, C.
Broad-spectrum allosteric inhibition of herpesvirus proteases
Biochemistry
53
4648-4660
2014
Human gammaherpesvirus 4, Human alphaherpesvirus 2, Human betaherpesvirus 5, Human gammaherpesvirus 8
brenda
Sabit, H.; Dahan, A.; Sun, J.; Provoda, C.J.; Lee, K.D.; Hilfinger, J.H.; Amidon, G.L.
Cytomegalovirus protease targeted prodrug development
Mol. Pharm.
10
1417-1424
2013
Human betaherpesvirus 5
brenda
Yang, K.; Wills, E.G.; Baines, J.D.
Release of the herpes simplex virus 1 protease by self cleavage is required for proper conformation of the portal vertex
Virology
429
63-73
2012
Herpes simplex virus
brenda
Zuehlsdorf, M.; Werten, S.; Klupp, B.G.; Palm, G.J.; Mettenleiter, T.C.; Hinrichs, W.
Dimerization-induced allosteric changes of the oxyanion-hole loop activate the pseudorabies virus assemblin pUL26N, a herpesvirus serine protease
PLoS Pathog.
11
e1005045
2015
Suid alphaherpesvirus 1 (Q83417), Suid alphaherpesvirus 1, Suid alphaherpesvirus 1 Kaplan (Q83417)
brenda
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