Adenain

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Adenain
Adenain
Identifiers
EC no.	3.4.22.39
CAS no.	369652-03-9
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

Adenain (EC 3.4.22.39) is an enzyme. This enzyme catalyses the following chemical 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)

This cysteine endopeptidase is encoded by adenoviruses.

References

↑ Webster A, Hay RT, Kemp G (January 1993). "The adenovirus protease is activated by a virus-coded disulphide-linked peptide". Cell. 72 (1): 97–104. doi:10.1016/0092-8674(93)90053-s. PMID 8422686.
↑ Ding J, McGrath WJ, Sweet RM, Mangel WF (April 1996). "Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor". The EMBO Journal. 15 (8): 1778–83. doi:10.1002/j.1460-2075.1996.tb00526.x. PMC 450093. PMID 8617222.
↑ Weber, J.M.; Rawlings, N.D.; Woessner, J.F. (1998). "Adenovirus protease". In Barrett, A.J. (ed.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 741–743.

External links

Adenain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Webster A, Hay RT, Kemp G (January 1993). "The adenovirus protease is activated by a virus-coded disulphide-linked peptide". Cell. 72 (1): 97–104. doi:10.1016/0092-8674(93)90053-s. PMID 8422686.

[2] Ding J, McGrath WJ, Sweet RM, Mangel WF (April 1996). "Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor". The EMBO Journal. 15 (8): 1778–83. doi:10.1002/j.1460-2075.1996.tb00526.x. PMC 450093. PMID 8617222.

[3] Weber, J.M.; Rawlings, N.D.; Woessner, J.F. (1998). "Adenovirus protease". In Barrett, A.J. (ed.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 741–743.

v t e Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain 3C-like protease Gingipain R Gingipain K

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)