ENZYME entry: EC 4.4.1.1
Accepted Name |
Cystathionine gamma-lyase.
|
Alternative Name(s) |
Cystathionase. |
Cystathioninase. |
Cysteine desulfhydrase. |
Cystine desulfhydrase. |
Gamma-cystathionase. |
Homoserine deaminase. |
Homoserine dehydratase. |
Reaction catalysed |
L-cystathionine + H(2)O <=> L-cysteine + NH(3) + 2-oxobutanoate |
Cofactor(s) |
Pyridoxal 5'-phosphate.
|
Comment(s) |
- The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an
unstable enamine product that tautomerizes to an imine form, which
undergoes a hydrolytic deamination to form 2-oxobutanoate and
ammonia.
- The latter reaction, which can occur spontaneously, can also be
catalyzed by EC 3.5.99.10.
- Also catalyzes the conversion of L-homoserine to 2-oxobutanoate and
ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of
L-cysteine to pyruvate, hydrogen sulfide and ammonia.
- Formerly EC 4.2.1.15.
|
Cross-references |
PROSITE | PDOC00677 |
BRENDA | 4.4.1.1 |
EC2PDB | 4.4.1.1 |
ExplorEnz | 4.4.1.1 |
PRIAM enzyme-specific profiles | 4.4.1.1 |
KEGG Ligand Database for Enzyme Nomenclature | 4.4.1.1 |
IUBMB Enzyme Nomenclature | 4.4.1.1 |
IntEnz | 4.4.1.1 |
MEDLINE | Find literature relating to 4.4.1.1 |
MetaCyc | 4.4.1.1 |
Rhea expert-curated reactions | 4.4.1.1 |
UniProtKB/Swiss-Prot |
P55216, CGL2_CAEEL; | F4K5T2, CGL_ARATH; | Q58DW2, CGL_BOVIN; |
Q55DV9, CGL_DICDI; | P32929, CGL_HUMAN; | Q60HG7, CGL_MACFA; |
Q8VCN5, CGL_MOUSE; | Q19QT7, CGL_PIG; | P18757, CGL_RAT; |
P31373, CYS3_YEAST; | Q59829, CYSA_STRCO; | O05394, MCCB_BACSU; |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 4.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-