Information on EC 3.4.22.39 - adenain

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The expected taxonomic range for this enzyme is: unidentified adenovirus

EC NUMBER
COMMENTARY
3.4.22.39
-
RECOMMENDED NAME
GeneOntology No.
adenain
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-/-Xaa- and -Yaa-Xaa-Gly-Xaa-/-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid)
show the reaction diagram
mechanism
-
Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-/-Xaa- and -Yaa-Xaa-Gly-Xaa-/-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid)
show the reaction diagram
consensus sequences
-
Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-/-Xaa- and -Yaa-Xaa-Gly-Xaa-/-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid)
show the reaction diagram
the GXG consensus site is cleaved more rapidly than the GGX site
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ad L3 23K proteinase
-
-
adenovirus endopeptidase
-
-
-
-
adenovirus type 2 protease
-
-
-
-
cysteine endopeptidase
-
-
-
-
cysteine endoprotease
-
-
-
-
cysteine peptidase
-
-
-
-
cysteine protease
-
-
-
-
cysteine proteinase
-
-
-
-
Endoprotease
-
-
-
-
L-cysteine proteinase
-
-
-
-
L3
-
-
-
-
L3/p23
-
-
-
-
Late L3 23 kDa protein
-
-
-
-
mercapto proteinase
-
-
-
-
oryzain
-
-
-
-
p23
-
-
-
-
papain-like cysteine protease
-
-
-
-
sulfhydryl esterase
-
-
-
-
sulfhydryl protease
-
-
-
-
sulfhydryl proteinase
-
-
-
-
thiol endopeptidase
-
-
-
-
thiol endoproteinase
-
-
-
-
thiol protease
-
-
-
-
thiol proteinase
-
-
-
-
thioprotease
-
-
-
-
trigger peptidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37353-41-6
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Ile-Arg-Gly-Gly-NH)2-rhodamine
?
show the reaction diagram
-
-
-
-
?
(Leu-Arg-Gly-Gly)2-rhodamine + H2O
?
show the reaction diagram
-
-
-
-
?
(Leu-Arg-Gly-Gly-NH)2-rhodamine + H2O
?
show the reaction diagram
human adenovirus
-
-
-
?
(Leu-Arg-Gly-Gly-NH)2-rhodamine + H2O
?
show the reaction diagram
human adenovirus
-
-
-
?
(Leu-Arg-Gly-Gly-NH)2-rhodamine + H2O
?
show the reaction diagram
human adenovirus
-
-
-
?
(N-carbobenzyloxy-Met-Arg-Gly-Gly-NH)2-rhodamine
?
show the reaction diagram
-
-
-
-
?
(N-carbobenzyloxy-Nle-Arg-Gly-Gly-NH)2-rhodamine
?
show the reaction diagram
-
-
-
-
?
(Nle-Arg-Gly-Gly-NH)2-rhodamine
?
show the reaction diagram
-
-
-
-
?
actin
36 kD protein
show the reaction diagram
-
-
-
?
core polypeptide PVII
polypeptide VII
show the reaction diagram
-
-
-
?
core polypeptide PVII
polypeptide VII
show the reaction diagram
-
-
-
?
core polypeptide PVII
polypeptide VII
show the reaction diagram
-
-
-
?
epsilon-N-5-carboxytetramethylrhodamine-Arg lucifer yellow CH hydrazone
?
show the reaction diagram
-
-
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Ser-Gly-Gly-Ala-Phe-Ser-Trp
Leu-Ser-Gly-Gly + Ala-Phe-Ser-Trp
show the reaction diagram
-
-
-
?
Ly-AnLRGA-GFSWK-ctmr-R
?
show the reaction diagram
-
-
-
-
?
Ly-AnLRGG-AFSWK-ctmr-R
?
show the reaction diagram
-
-
-
-
?
Met-Glu-Gly-Gly-Ala-Lys-Lys
?
show the reaction diagram
-
-
-
-
?
Met-Phe-Gly-Gly-Ala-Lys-Lys-Arg
?
show the reaction diagram
-
-
-
-
?
ovalbumin
37 kD protein
show the reaction diagram
-
-
-
?
preterminal proteins
?
show the reaction diagram
-
pVI, pVII, pVIII, IIIa, 11K
-
-
-
pVI
protein VI
show the reaction diagram
-
-
-
?
rhodamine 1,10-bis-(L-leucyl-L-arginylglycylglycine amide) tetrahydrochloride
?
show the reaction diagram
-
-
-
-
-
rhodamine 1,10-bis-(L-leucyl-L-arginylglycylglycine amide) tetrahydrochloride
?
show the reaction diagram
-
-
-
-
?
Met-Ser-Gly-Gly-Ala-Phe-Ser-Trp
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme can function as deubiquitinating enzyme in vitro and in vivo. The protein deubiquitination can be as efficient as proteolytic processing of viral proteins
-
?
additional information
?
-
-
required for the synthesis of infectious virus and is a target for antiviral therapy
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
preterminal proteins
?
show the reaction diagram
-
pVI, pVII, pVIII, IIIa, 11K
-
-
-
additional information
?
-
-
the enzyme can function as deubiquitinating enzyme in vitro and in vivo. The protein deubiquitination can be as efficient as proteolytic processing of viral proteins
-
?
additional information
?
-
-
required for the synthesis of infectious virus and is a target for antiviral therapy
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-(hydroxynitrosohydrazono)bis-ethaneamine
-
NO generated from 2,2'-(hydroxynitrosohydrazono)bis-ethaneamine inhibits
4,4-dithiodipyridine
-
-
bestatin, L-transepoxy-succinyl-leucylamido-(4-guanido)-butane
-
-
-
bestatin, L-transepoxy-succinyl-leucylamido-(4-guanido)-butane tyrosine
-
-
-
glutamic acid
-
inhibition by displacement of viral DNA from complexes with enzyme
N-[4-[1-(3-aminopropyl)-2-hydroxy-2-nitrosohydrazino]butyl]-1,3-propanediamine
-
NO generated from N-[4-[1-(3-aminopropyl)-2-hydroxy-2-nitrosohydrazino]butyl]-1,3-propanediamine inhibits the enzyme
NaCl
-
inhibition by displacement of viral DNA from complexes with enzyme
NO
-
inhibits adenovirus replication by targeting the adenovirus proteinase, inhibition is reversible with dithiothreitol
p-chloromercuribenzoate
-
-
Phenylmethylsulfonylfluoride
-
-
Soybean trypsin inhibitor
-
-
-
tosyl-lysinechloromethyl ketone
-
-
tosylamide phenylethylchloromethyl ketone
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
activation
EDTA
-
stimulation
GVQSLKRRRCF
-
pVIc; required
GVQSLKRRRCF
-
pVI-CT, disulfide-linked; required
GVQSLKRRRCF
-
required
polyE
-
interaction of enzyme-virion precursor protein pVI with polymers of glutamic acid leads to increase in substrate hydrolysis
-
pVIc
human adenovirus
-
the enzyme requires two cofactors for maximal activity,the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA. Influence of mutant pVIcs on Km-value and turnover number with (Leu-Arg-Gly-Gly-NH)2-rhodamine as substrate
pVIc
human adenovirus
-
the enzyme requires two cofactors for maximal activity,the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA
pVIc
human adenovirus
-
11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA is required as cofactor
pVIc
-
enzyme is stimulated by the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein. In virus particles the enzyme is linked to pVIc via a disulfide bond
viral DNA
-
not required in vitro
-
viral DNA
-
required
-
viral DNA
human adenovirus
-
the enzyme requires two cofactors for maximal activity, the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA
-
virion precursor protein pVI
-
11 acid peptide
-
virion precursor protein pVI
-
11 acid peptide. Conserved basic motif KRRR of peptide is less important than the N- or C-terminal regions of peptide in formation of the enzyme-peptide heterodimer and in the activity of the complex. Motif acts as nuclear localization signal
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00517
(Ile-Arg-Gly-Gly-NH)2-rhodamine
-
-
-
0.0034
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, activation by viral DNA and the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA
0.0092
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, activation by viral DNA
0.0099
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, activation by the the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA
0.0948
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, in absence of any cofactor
0.00474
(N-carbobenzyloxy-Met-Arg-Gly-Gly-NH)2-rhodamine
-
-
-
0.000758
(N-carbobenzyloxy-Nle-Arg-Gly-Gly-NH)2-rhodamine
-
-
-
0.0014
rhodamine 110,bis-(L-leucyl-L-arginylglycylglycine amide),tetrahydrochloride
-
-
0.00183
rhodamine 110,bis-(L-leucyl-L-arginylglycylglycine amide),tetrahydrochloride
-
-
0.005
rhodamine 110,bis-(L-leucyl-L-arginylglycylglycine amide),tetrahydrochloride
-
-
0.0024
(Nle-Arg-Gly-Gly-NH)2-rhodamine
-
-
-
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
human adenovirus
-
influence of mutant pVIcs on Km-value with (Leu-Arg-Gly-Gly-NH)2-rhodamine as substrate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, in absence of any cofactor
0.0248
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, activation by viral DNA
0.271
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, activation by the the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA
2.78
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, activation by viral DNA and the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA
3 - 6
(Leu-Arg-Gly-Gly-NH)2-rhodamine
human adenovirus
-
pH 8.0, 25C, activation by viral DNA and the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA
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
human adenovirus
-
influence of mutant pVIcs on turnover number with (Leu-Arg-Gly-Gly-NH)2-rhodamine as substrate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00023
glutamic acid
-
37C, pH 8.0
0.000329
NaCl
-
37C, pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
HeLa cell infected with adenovirus type 2
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Human adenovirus C serotype 2
Human adenovirus C serotype 2
Human adenovirus C serotype 2
Human adenovirus C serotype 2
Human adenovirus C serotype 2
Human adenovirus D serotype 8
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
-
gel filtration, SDS-PAGE
36695
25500
-
gel filtration, SDS-PAGE
36695
25500
-
-
36710
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 20000, SDS-PAGE, gel filtration
monomer
-
1 * 25500, SDS-PAGE, gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure at 1.6-A resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor
human adenovirus
-
hanging-drop vapour-diffusion technique
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Sf9/baculovirus cells
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Sf9/baculovirus cells
-
glutathione S-transferase-fusion protein expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
NO may be a useful antiadenovirus agent, inhibits adenovirus replication by targeting the adenovirus proteinase. Treatment of infectious virus by 2,2'-(hydroxynitrosohydrazono)bis-ethaneamine dramatically decreases viral infectivity
medicine
-
required for the synthesis of infectious virus and is a target for antiviral therapy