3.4.22.39: adenain

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

Reaction

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) =

Synonyms

Ad L3 23K proteinase, adenain 5, adenain 8, adenoviral protease, adenovirus endopeptidase, adenovirus proteinase, adenovirus type 2 protease, AVP, AVP5, AVP8, 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

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.22 Cysteine endopeptidases

                3.4.22.39 adenain

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Results	in table
34	Activating Compound
353	AA Sequence
2	Application
1	CAS Registry Number
10	Cloned(Commentary)
4	Crystallization (Commentary)
19	IC50 Value
41	Inhibitors
3	Ki Value [mM]
12	KM Value [mM]
2	Localization
5	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
33	Organism
7	PDB ID
1	pH Optimum
1	pH Range
1	Protein Variants
7	Purification (Commentary)
8	Reaction
1	Reaction Type
32	Reference
1	Source Tissue
1	Specific Activity [micromol/min/mg]
36	Substrates and Products (Substrate)
4	Subunits
39	Synonyms
7	Turnover Number [1/s]

Activating Compound

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Activating Compound on EC 3.4.22.39 - adenain

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

cysteine

unidentified adenovirus

-

activation

36701, 36702

DNA

3 entries

DTT

unidentified adenovirus

-

activation

36701, 36707, 36711

EDTA

unidentified adenovirus

-

stimulation

36702

GVQSLKRRRCF

3 entries

peptide VIc

Human adenovirus sp.

-

an 11-amino acid peptide (GVQSLKRRRCF) originating from the C terminus of the precursor protein pVI

732108

-

polyE

unidentified adenovirus

-

interaction of enzyme-virion precursor protein pVI with polymers of glutamic acid leads to increase in substrate hydrolysis

667686

-

pVIc

7 entries

viral DNA

4 entries

-

virion precursor protein pVI

2 entries

-

DNA

Human adenovirus sp.

-

DNA binding of pVI is the first step in the activation of adenovirus proteinase. The relative kcat/Km is enhanced 110fold in the presence of DNA. When pVIc and DNA are bound to the enzyme, the kcat/Km increases synergistically by 16000fold

732107

DNA

Human adenovirus sp.

-

the enzyme is partially activated by being bound to viral DNA

732108, 732110

DNA

Human adenovirus sp.

P03252

viral DNA

732109

GVQSLKRRRCF

unidentified adenovirus

-

required

36701, 36702, 36704, 36707, 36709

GVQSLKRRRCF

unidentified adenovirus

-

pVI-CT, disulfide-linked

36704, 36707

GVQSLKRRRCF

unidentified adenovirus

-

pVIc

36702

pVIc

Human adenovirus sp.

-

11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA is required as cofactor

650412

pVIc

Human adenovirus sp.

-

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

650032

pVIc

Human adenovirus sp.

-

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

650027

pVIc

Human adenovirus sp.

P03252

11-amino acid peptide from the C terminus of adenovirus precursor protein pVI with sequence GVQSLKRRRCF

732109

pVIc

Human adenovirus sp.

-

the C terminus of pVI (GVQSLKRRRCF) activates the adenovirus proteinase. The relative kcat/Km is enhanced 1130fold in the presence of pVIc. When pVIc and DNA are bound to the enzyme, the kcat/Km increases synergistically by 16000fold

732107

pVIc

Human adenovirus sp.

-

the enzyme can be activated by pVIc (GVQSLKRRRCF) to form the enzyme-pVIc complex in the core of the immature virion

732110

pVIc

unidentified adenovirus

-

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

654014

viral DNA

Human adenovirus sp.

-

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

650032

-

viral DNA

unidentified adenovirus

-

-

667686

-

viral DNA

unidentified adenovirus

-

required

36702, 36709

-

viral DNA

unidentified adenovirus

-

not required in vitro

36707

-

virion precursor protein pVI

unidentified adenovirus

-

11 acid peptide

667686

-

virion precursor protein pVI

unidentified adenovirus

-

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

669684

-