| alliin lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.4.1.4 | ||||||||
| CAS no. | 9031-77-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Alliinase_C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of alliinase from garlic- apo form | |||||||||
| Identifiers | |||||||||
| Symbol | Alliinase_C | ||||||||
| Pfam | PF04864 | ||||||||
| Pfam clan | CL0061 | ||||||||
| InterPro | IPR006948 | ||||||||
| SCOP2 | 1lk9 / SCOPe / SUPFAM | ||||||||
| |||||||||
| Alliinase EGF-like domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
crystal structure of alliinase from garlic- apo form | |||||||||
| Identifiers | |||||||||
| Symbol | EGF_alliinase | ||||||||
| Pfam | PF04863 | ||||||||
| Pfam clan | CL0001 | ||||||||
| InterPro | IPR006947 | ||||||||
| SCOP2 | 1lk9 / SCOPe / SUPFAM | ||||||||
| |||||||||
In enzymology, an alliin lyase (EC 4.4.1.4) is an enzyme that catalyzes the chemical reaction
- an S-alkyl-L-cysteine S-oxide an alkyl sulfenate + 2-aminoacrylate
Hence, this enzyme has one substrate, S-alkyl-L-cysteine S-oxide, and two products, alkyl sulfenate and 2-aminoacrylate.
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is S-alkyl-L-cysteine S-oxide alkyl-sulfenate-lyase (2-aminoacrylate-forming). Other names in common use include alliinase, cysteine sulfoxide lyase, alkylcysteine sulfoxide lyase, S-alkylcysteine sulfoxide lyase, L-cysteine sulfoxide lyase, S-alkyl-L-cysteine sulfoxide lyase, and alliin alkyl-sulfenate-lyase. It employs one cofactor, pyridoxal phosphate.
Many alliinases contain a novel N-terminal epidermal growth factor-like domain (EGF-like domain).[1]
- ^ Kuettner EB, Hilgenfeld R, Weiss MS (November 2002). "The active principle of garlic at atomic resolution". J. Biol. Chem. 277 (48): 46402–7. doi:10.1074/jbc.M208669200. PMID 12235163.