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Literature summary for 3.5.4.17 extracted from

  • Uchida, H.; Narita, Y.; Masuda, A.; Chen, Y.X.; Nomura, A.
    Recognition of ribose moiety by adenosine (phosphate) deaminase from squid liver (1995), Biosci. Biotechnol. Biochem., 59, 2120-2122.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
3'-IMP competitive inhibition of deamination of adenosine 3'-phenylphosphonate Todarodes pacificus
adenine competitive inhibition of deamination of adenosine 3'-phenylphosphonate Todarodes pacificus
Inosine competitive inhibition of deamination of adenosine 3'-phenylphosphonate Todarodes pacificus
purine riboside competitive inhibition of deamination of adenosine 3'-phenylphosphonate Todarodes pacificus

Organism

Organism UniProt Comment Textmining
Todarodes pacificus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Todarodes pacificus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Todarodes pacificus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2',3'-cAMP + H2O
-
Todarodes pacificus 2',3'-cIMP + NH3
-
?
2'-deoxyadenosine + H2O
-
Todarodes pacificus 2'-deoxyinosine + NH3
-
?
3'-deoxyadenosine + H2O
-
Todarodes pacificus 3'-deoxyinosine + NH3
-
?
5'-deoxyadenosine + H2O the enzyme shows much lower activity with 5'-deoxyadenosine than with 2'-deoxyadenosine or 3'-deoxyadenosine Todarodes pacificus 5'-deoxyinosine + NH3
-
?
adenosine + H2O
-
Todarodes pacificus inosine + NH3
-
?
adenosine 3'-phenyl phosphonate + H2O
-
Todarodes pacificus inosine 3'-phenylphosphonate + NH3
-
?
ApA + H2O 37.6% of the activity with 2',3'-cAMP Todarodes pacificus IpI + NH3
-
?
ApC + H2O 41.8% of the activity with 2',3'-cAMP Todarodes pacificus IpC + NH3
-
?
ApCpC + H2O 12.1% of the activity with 2',3'-cAMP Todarodes pacificus IpCpC + NH3
-
?
ApG + H2O 30.9% of the activity with 2',3'-cAMP Todarodes pacificus IpG + NH3
-
?
ApU + H2O 51.5% of the activity with 2',3'-cAMP Todarodes pacificus IpU + NH3
-
?
additional information the enzyme deaminates 5'-hydroxyl terminal adenosine residues in dinucleotides and trinucleotides, but not the 3'-hydroxyl terminal one in dinucleotides. The 5'-hydroxyl group of the ribose moiety is necessary for the substrate binding and catalytic activity of the squid enzyme Todarodes pacificus ?
-
?