|
Enzyme - EC 3.3.1.1 - Adenosylhomocysteinase
|
|||||
|
|||||
|
Click on the image to start downloading the PDB file (tridimensional and interactive). |
|||||
|
Dados da estrutura
|
Unidade biológica: Homotetrâmero
|
||||
|
|
|||||
|
EC
|
3.3.1.1
|
||||
|
Official Name
|
Adenosylhomocysteinase
|
||||
|
Alternative Name(s)
|
S-adenosyl-L-homocysteine hydrolase
|
||||
|
Class
|
3.Hydrolases
3.Acting on ether bonds 1.Thioether hydrolases |
||||
|
Catalysed reaction
|
S-adenosyl-L-homocysteine + H2O
|
||||
|
Substrates
|
S-adenosyl-L-homocysteine
H2O |
||||
|
Products
|
adenosine L-homocysteine |
||||
|
Cofactor(s)
|
NAD+
|
||||
|
Metabolic Pathways
|
|||||
|
Other comments
|
S-adenosyl-L-homocysteine hydrolase (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydratation of S-adenosyl-L-homocysteine into adenosine and homocysteine. AdoHcyase is an ubiquitous enzyme which binds and requires NAD+ as a cofactor. |
||||
|
AdoHcyase is a highly conserved protein of about 430 to 470 amino acids.
As signature patterns, it has been selected two highly conserved regions. The first
pattern is located in the N-terminal section; the second is derived from a
glycine-rich region in the central part of AdoHcyase; a region thought to be
involved in NAD-binding. |
|||||
|
|
|||||