CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.640 | Aspartate Aminotransferase; domain 2 |
|
3.40.640.10 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
Domain Context
CATH Clusters
| Superfamily | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
| Functional Family | Cystathionine beta-lyase |
Enzyme Information
| 4.4.1.28 |
L-cysteine desulfidase.
based on mapping to UniProt P06721
L-cysteine + H(2)O = sulfide + NH(3) + pyruvate.
-!- The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1). -!- It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The same reaction can also be catalyzed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1).
|
| 4.4.1.13 |
Cysteine-S-conjugate beta-lyase.
based on mapping to UniProt P06721
An L-cysteine-S-conjugate + H(2)O = RSH + NH(3) + pyruvate.
-!- A pyridoxal 5'-phosphate protein. -!- The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions. -!- The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases. -!- Formerly EC 4.4.1.6 and EC 4.4.1.8.
|
UniProtKB Entries (1)
| P06721 |
METC_ECOLI
Escherichia coli K-12
Cystathionine beta-lyase MetC
|
PDB Structure
| PDB | 1CL2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study.
Biochemistry
|
