Description
Enzyme in vertebrates which catabolizes S-adenosyl-L-homocysteine.
Appearance
White powder, lyophilized
Product Overview
S-adenosyl-L-homocysteine hydrolase (SAHH, EC 3.3.1.1) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. SAHH is a ubiquitous enzyme which binds and requires NAD+ as a cofactor. AdoHcyase is a highly conserved protein of about 430 to 470 amino acids. The family contains a glycine-rich region in the central part of AdoHcyase; aregion thought to be involved in NAD-binding. This protein may use themorpheein model of allosteric regulation.
Enzyme Commission Number
EC 3.3.1.1
Molecular Weight
About 44kDa (SDS-PAGE detection)
Purity
>90% (SDS-PAGE test)
Unit Definition
One unit will catalyze 1.0 μmole of S-adenosyl-L-homocysteine to adenosine and Hcy per min at pH 7.4 at 37°C.
Storage
Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles.
Buffer
Tris buffer, pH8.0
Synonyms
Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1
