DB code: M00167
| RLCP classification | 1.13.30000.10 : Hydrolysis | |
|---|---|---|
| CATH domain | 3.30.300.50 : GMP Synthetase; Chain A, domain 3 | |
| 3.30.300.50 : GMP Synthetase; Chain A, domain 3 | ||
| 2.40.10.10 : Thrombin, subunit H | Catalytic domain | |
| 2.40.10.10 : Thrombin, subunit H | Catalytic domain | |
| E.C. | 3.4.21.12 | |
| CSA | 2lpr | |
| M-CSA | 2lpr | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 2.40.10.10 : Thrombin, subunit H | M00139 D00214 D00426 M00133 D00428 D00429 D00430 D00431 D00432 D00433 D00434 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00217 M00216 D00528 D00848 D00850 D00851 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | MEROPS | Pfam |
|---|---|---|---|---|
| P00778 |
Alpha-lytic protease
|
EC
3.4.21.12
Alpha-lytic endopeptidase |
S01.268
(Serine)
|
PF02983
(Pro_Al_protease)
PF00089 (Trypsin) [Graphical View] |
| KEGG enzyme name |
|---|
|
alpha-lytic endopeptidase
myxobacter alpha-lytic proteinase alpha-lytic proteinase alpha-lytic protease Mycobacterium sorangium alpha-lytic proteinase Myxobacter 495 alpha-lytic proteinase alpha-lytic proteinase Myxobacter alpha-lytic proteinase Mycobacterium sorangium alpha-lytic proteinase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P00778 | PRLA_LYSEN | Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||||||
| KEGG-id | C00012 | C02065 | C00001 | C00012 | C00098 | I00087 | I00085 | I00086 | |||||
| E.C. | |||||||||||||
| Compound | Peptide | Protein alanine | H2O | Peptide | Oligopeptide | Peptidyl-tetrahedral intermediate | Acyl-enzyme | Tetrahedral intermediate | |||||
| Type | peptide/protein | peptide/protein | H2O | peptide/protein | amine group,carboxyl group,peptide/protein | ||||||||
| ChEBI |
15377 15377 |
||||||||||||
| PubChem |
22247451 962 22247451 962 |
||||||||||||
| 2proA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2proB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2proC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3proC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3proD01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4proC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4proD01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2proA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2proB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2proC02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3proC02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3proD02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4proC02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4proD02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1boqA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbaA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbbA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbcA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbdA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbeA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbfA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbhA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbiA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbjA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbkA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gblA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbmA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p01A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p02A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p03A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p04A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p05A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p06A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p09A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p10A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p11E01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p12E01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qq4A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qrwA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qrxA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1talA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2alpA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2lprA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2ullA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3lprA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3proA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3proB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4proA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4proB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 5lprA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 6lprA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 7lprA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 8lprA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 9lprA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1boqA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbaA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbbA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2A (chain P) | |
| 1gbcA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-BLE (chain P) | |
| 1gbdA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2F (chain P) | |
| 1gbeA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbfA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2A (chain P) | |
| 1gbhA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-BLE (chain P) | |
| 1gbiA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:ALA-ALA-PRO-B2F (chain P) | Unbound | |
| 1gbjA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gbkA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2A (chain P) | |
| 1gblA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-BLE (chain P) | |
| 1gbmA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2F (chain P) | |
| 1p01A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:BOC-ALA-PRO-B2V (chain P) | |
| 1p02A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2A (chain P) | |
| 1p03A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2V (chain P) | |
| 1p04A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2I (chain P) | |
| 1p05A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-BNO (chain P) | |
| 1p06A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:ALA-ALA-PRO-B2F (chain P) | Unbound | |
| 1p09A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1p10A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2V (chain P) | |
| 1p11E02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:BOC-ALA-ALA-PRO-PVA-LAC-ALA (chain P), BOC-ALA-ALA-PRO-PVA (chain I) | |
| 1p12E02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:BOC-ALA-ALA-PRO-PVA-LAC-ALA (chain I) | Unbound | |
| 1qq4A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qrwA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qrxA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1talA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2alpA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2lprA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2V (chain P) | |
| 2ullA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3lprA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-BNO (chain P) | |
| 3proA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:2AB | |
| 3proB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:2AB | |
| 4proA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4proB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 5lprA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2A (chain P) | |
| 6lprA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-BNO (chain P) | |
| 7lprA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-BLE (chain P) | |
| 8lprA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-B2F (chain P) | |
| 9lprA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:ALA-ALA-PRO-BLE (chain P) | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P00778 | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 2proA01 |
|
|
|
|
|
|||||
| 2proB01 |
|
|
|
|
|
|||||
| 2proC01 |
|
|
|
|
|
|||||
| 3proC01 |
|
|
|
|
|
|||||
| 3proD01 |
|
|
|
|
|
|||||
| 4proC01 |
|
|
|
|
|
|||||
| 4proD01 |
|
|
|
|
|
|||||
| 2proA02 |
|
|
|
|
|
|||||
| 2proB02 |
|
|
|
|
|
|||||
| 2proC02 |
|
|
|
|
|
|||||
| 3proC02 |
|
|
|
|
|
|||||
| 3proD02 |
|
|
|
|
|
|||||
| 4proC02 |
|
|
|
|
|
|||||
| 4proD02 |
|
|
|
|
|
|||||
| 1boqA01 |
|
|
|
|
|
HIS 36;ASP 63 | ||||
| 1gbaA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbbA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbcA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbdA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbeA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbfA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbhA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbiA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbjA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbkA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gblA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1gbmA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p01A01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p02A01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p03A01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p04A01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p05A01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p06A01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p09A01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p10A01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p11E01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1p12E01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1qq4A01 |
|
|
|
|
|
HIS 36;ASP 63 | ||||
| 1qrwA01 |
|
|
|
|
|
HIS 36;ASP 63 | ||||
| 1qrxA01 |
|
|
|
|
|
HIS 36;ASP 63 | ||||
| 1talA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 2alpA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 2lprA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 2ullA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 3lprA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 3proA01 |
|
|
|
|
|
HIS 36;ASP 63 | ||||
| 3proB01 |
|
|
|
|
|
HIS 36;ASP 63 | ||||
| 4proA01 |
|
|
|
|
|
HIS 36;ASP 63 | ||||
| 4proB01 |
|
|
|
|
|
HIS 36;ASP 63 | ||||
| 5lprA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 6lprA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 7lprA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 8lprA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 9lprA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1boqA02 |
|
|
|
|
|
SER 143 | GLY 141;SER 143 | |||
| 1gbaA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A, G216A | ||
| 1gbbA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A, G216A | ||
| 1gbcA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A, G216A | ||
| 1gbdA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A, G216A | ||
| 1gbeA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A, G216L | ||
| 1gbfA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A, G216L | ||
| 1gbhA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A, G216L | ||
| 1gbiA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A, G216L | ||
| 1gbjA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A | ||
| 1gbkA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A | ||
| 1gblA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A | ||
| 1gbmA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M190A | ||
| 1p01A02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1p02A02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1p03A02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1p04A02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1p05A02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1p06A02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1p09A02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M213A | ||
| 1p10A02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M213A | ||
| 1p11E02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1p12E02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 1qq4A02 |
|
|
|
|
|
SER 143 | GLY 141;SER 143 | mutant R102H, G134S | ||
| 1qrwA02 |
|
|
|
|
|
SER 143 | GLY 141;SER 143 | mutant R102H, G134S | ||
| 1qrxA02 |
|
|
|
|
|
SER 143 | GLY 141;SER 143 | |||
| 1talA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 2alpA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 2lprA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M192A | ||
| 2ullA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| 3lprA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M192A | ||
| 3proA02 |
|
|
|
|
|
SER 143 | GLY 141;SER 143 | mutant M158A | ||
| 3proB02 |
|
|
|
|
|
SER 143 | GLY 141;SER 143 | mutant M158A | ||
| 4proA02 |
|
|
|
|
|
SER 143 | GLY 141;SER 143 | mutant M158A | ||
| 4proB02 |
|
|
|
|
|
SER 143 | GLY 141;SER 143 | mutant M158A | ||
| 5lprA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M213A | ||
| 6lprA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M213A | ||
| 7lprA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M213A | ||
| 8lprA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | mutant M213A | ||
| 9lprA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[1]
|
equation (1), equation (2), equation (3), equation (4), p.768-771 | |
|
[4]
|
Fig.1, p.424-428 | |
|
[9]
|
Fig.6, p.7613-7614 | |
|
[10]
|
p.7695-7696 | |
|
[37]
|
Fig.3, p.10374-10376 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 117110 |
| Journal | J Mol Biol |
| Year | 1979 |
| Volume | 131 |
| Pages | 743-75 |
| Authors | Brayer GD, Delbaere LT, James MN |
| Title | Molecular structure of the alpha-lytic protease from Myxobacter 495 at 2.8 Angstroms resolution. |
| Related PDB | |
| Related UniProtKB | P00778 |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6769571 |
| Journal | Can J Biochem |
| Year | 1980 |
| Volume | 58 |
| Pages | 252-71. |
| Authors | James MN |
| Title | An X-ray crystallographic approach to enzyme structure and function. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7038675 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1981 |
| Volume | 78 |
| Pages | 7323-6 |
| Authors | Bachovchin WW, Kaiser R, Richards JH, Roberts JD |
| Title | Catalytic mechanism of serine proteases: reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7049067 |
| Journal | Annu Rev Biophys Bioeng |
| Year | 1982 |
| Volume | 11 |
| Pages | 419-44 |
| Authors | Steitz TA, Shulman RG |
| Title | Crystallographic and NMR studies of the serine proteases. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6802183 |
| Journal | Biochim Biophys Acta |
| Year | 1982 |
| Volume | 702 |
| Pages | 105-11 |
| Authors | Recchia J, Matthews CR, Rhee MJ, Horrocks WD Jr |
| Title |
Interresidue distance measurements in proteins. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6395886 |
| Journal | Biochemistry |
| Year | 1984 |
| Volume | 23 |
| Pages | 5933-7 |
| Authors | Huang TH, Bachovchin WW, Griffin RG, Dobson CM |
| Title |
High-resolution nitrogen-15 nuclear magnetic resonance studies of alpha-lytic protease in solid state. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 3900416 |
| Journal | J Mol Biol |
| Year | 1985 |
| Volume | 184 |
| Pages | 479-502 |
| Authors | Fujinaga M, Delbaere LT, Brayer GD, James MN |
| Title |
Refined structure of alpha-lytic protease at 1.7 A resolution. |
| Related PDB | 2alp |
| Related UniProtKB | P00778 |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3934665 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1985 |
| Volume | 82 |
| Pages | 7948-51 |
| Authors | Bachovchin WW |
| Title | Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 3122831 |
| Journal | Biochemistry |
| Year | 1987 |
| Volume | 26 |
| Pages | 7609-14 |
| Authors | Bone R, Shenvi AB, Kettner CA, Agard DA |
| Title | Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid. |
| Related PDB | 1p01 |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3207700 |
| Journal | Biochemistry |
| Year | 1988 |
| Volume | 27 |
| Pages | 7689-97 |
| Authors | Bachovchin WW, Wong WY, Farr-Jones S, Shenvi AB, Kettner CA |
| Title | Nitrogen-15 NMR spectroscopy of the catalytic-triad histidine of a serine protease in peptide boronic acid inhibitor complexes. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 2611204 |
| Journal | Biochemistry |
| Year | 1989 |
| Volume | 28 |
| Pages | 7600-9 |
| Authors | Bone R, Frank D, Kettner CA, Agard DA |
| Title | Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates. |
| Related PDB | 1p02 1p03 1p04 1p05 1p06 |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2646278 |
| Journal | J Bacteriol |
| Year | 1989 |
| Volume | 171 |
| Pages | 1320-5 |
| Authors | Silen JL, Frank D, Fujishige A, Bone R, Agard DA |
| Title | Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 2716847 |
| Journal | Nature |
| Year | 1989 |
| Volume | 339 |
| Pages | 191-5 |
| Authors | Bone R, Silen JL, Agard DA |
| Title | Structural plasticity broadens the specificity of an engineered protease. |
| Related PDB | 1p09 1p10 |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2223778 |
| Journal | Biochemistry |
| Year | 1990 |
| Volume | 29 |
| Pages | 7468-74 |
| Authors | Brothers HM 2nd, Kostic NM |
| Title | Catalytic activity of the serine proteases alpha-chymotrypsin and alpha-lytic protease tagged at the active site with a (terpyridine)platinum(II) chromophore. |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 1931963 |
| Journal | Biochemistry |
| Year | 1991 |
| Volume | 30 |
| Pages | 10388-98 |
| Authors | Bone R, Fujishige A, Kettner CA, Agard DA |
| Title | Structural basis for broad specificity in alpha-lytic protease mutants. |
| Related PDB | 2lpr 3lpr 5lpr 6lpr 7lpr 8lpr 9lpr |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 1998685 |
| Journal | Biochemistry |
| Year | 1991 |
| Volume | 30 |
| Pages | 2263-72 |
| Authors | Bone R, Sampson NS, Bartlett PA, Agard DA |
| Title | Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters. |
| Related PDB | 1p11 1p12 |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1856870 |
| Journal | J Mol Biol |
| Year | 1991 |
| Volume | 220 |
| Pages | 495-506 |
| Authors | Wilson C, Mace JE, Agard DA |
| Title | Computational method for the design of enzymes with altered substrate specificity. |
| Related PDB | |
| Related UniProtKB | |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1896427 |
| Journal | Proteins |
| Year | 1991 |
| Volume | 10 |
| Pages | 140-8 |
| Authors | Caldwell JW, Agard DA, Kollman PA |
| Title | Free energy calculations on binding and catalysis by alpha-lytic protease: the role of substrate size in the P1 pocket. |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1445861 |
| Journal | Biochemistry |
| Year | 1992 |
| Volume | 31 |
| Pages | 11216-23 |
| Authors | Epstein DM, Abeles RH |
| Title |
Role of serine 214 and tyrosine 171, |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8251483 |
| Journal | Biochemistry |
| Year | 1993 |
| Volume | 32 |
| Pages | 12651-5 |
| Authors | Tsilikounas E, Kettner CA, Bachovchin WW |
| Title |
11B NMR spectroscopy of peptide boronic acid inhibitor complexes of alpha-lytic protease. |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8445659 |
| Journal | J Mol Biol |
| Year | 1993 |
| Volume | 229 |
| Pages | 996-1006 |
| Authors | Wilson C, Gregoret LM, Agard DA |
| Title | Modeling side-chain conformation for homologous proteins using an energy-based rotamer search. |
| Related PDB | |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7944385 |
| Journal | Arch Biochem Biophys |
| Year | 1994 |
| Volume | 314 |
| Pages | 132-41 |
| Authors | Haggett KD, Graham LD, Milner SJ, Whittaker RG |
| Title | Purification and characterization of S1 mutants of alpha-lytic protease having altered catalytic properties. |
| Related PDB | |
| Related UniProtKB | |
| [23] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8155642 |
| Journal | Biochemistry |
| Year | 1994 |
| Volume | 33 |
| Pages | 4251-7 |
| Authors | Schellenberger V, Turck CW, Rutter WJ |
| Title |
Role of the S' subsites in serine protease catalysis. |
| Related PDB | |
| Related UniProtKB | |
| [24] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 7500345 |
| Journal | J Mol Biol |
| Year | 1995 |
| Volume | 254 |
| Pages | 720-36 |
| Authors | Mace JE, Agard DA |
| Title | Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. |
| Related PDB | 1gba 1gbb 1gbc 1gbd 1gbe 1gbf 1gbh 1gbi 1gbj 1gbk 1gbl 1gbm |
| Related UniProtKB | |
| [25] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7643381 |
| Journal | J Mol Biol |
| Year | 1995 |
| Volume | 251 |
| Pages | 116-34 |
| Authors | Mace JE, Wilk BJ, Agard DA |
| Title | Functional linkage between the active site of alpha-lytic protease and distant regions of structure: scanning alanine mutagenesis of a surface loop affects activity and substrate specificity. |
| Related PDB | |
| Related UniProtKB | |
| [26] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9092819 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 3894-902 |
| Authors | Sohl JL, Shiau AK, Rader SD, Wilk BJ, Agard DA |
| Title | Inhibition of alpha-lytic protease by pro region C-terminal steric occlusion of the active site. |
| Related PDB | |
| Related UniProtKB | |
| [27] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9335113 |
| Journal | J Biomol NMR |
| Year | 1997 |
| Volume | 10 |
| Pages | 21-7 |
| Authors | Davis JH, Agard DA, Handel TM, Basus VJ |
| Title | Alterations in chemical shifts and exchange broadening upon peptide boronic acid inhibitor binding to alpha-lytic protease. |
| Related PDB | |
| Related UniProtKB | |
| [28] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 9232638 |
| Journal | Protein Sci |
| Year | 1997 |
| Volume | 6 |
| Pages | 1375-86 |
| Authors | Rader SD, Agard DA |
| Title | Conformational substates in enzyme mechanism: the 120 K structure of alpha-lytic protease at 1.5 A resolution. |
| Related PDB | 1tal 2ull |
| Related UniProtKB | |
| [29] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9353195 |
| Journal | Science |
| Year | 1997 |
| Volume | 278 |
| Pages | 1128-32 |
| Authors | Ash EL, Sudmeier JL, De Fabo EC, Bachovchin WW |
| Title | A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment. |
| Related PDB | |
| Related UniProtKB | |
| [30] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9601029 |
| Journal | Biochemistry |
| Year | 1998 |
| Volume | 37 |
| Pages | 7696-707 |
| Authors | Davis JH, Agard DA |
| Title | Relationship between enzyme specificity and the backbone dynamics of free and inhibited alpha-lytic protease. |
| Related PDB | |
| Related UniProtKB | |
| [31] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 9724517 |
| Journal | Biochemistry |
| Year | 1998 |
| Volume | 37 |
| Pages | 12058-67 |
| Authors | Peters RJ, Shiau AK, Sohl JL, Anderson DE, Tang G, Silen JL, Agard DA |
| Title | Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease. |
| Related PDB | 1boq |
| Related UniProtKB | P00778 |
| [32] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 9808037 |
| Journal | Nat Struct Biol |
| Year | 1998 |
| Volume | 5 |
| Pages | 945-50 |
| Authors | Sauter NK, Mau T, Rader SD, Agard DA |
| Title | Structure of alpha-lytic protease complexed with its pro region. |
| Related PDB | 2pro 3pro 4pro |
| Related UniProtKB | P00778 |
| [33] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9796818 |
| Journal | Nature |
| Year | 1998 |
| Volume | 395 |
| Pages | 817-9 |
| Authors | Sohl JL, Jaswal SS, Agard DA |
| Title | Unfolded conformations of alpha-lytic protease are more stable than its native state. |
| Related PDB | |
| Related UniProtKB | |
| [34] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9931265 |
| Journal | J Mol Biol |
| Year | 1999 |
| Volume | 286 |
| Pages | 267-78 |
| Authors | Miller DW, Agard DA |
| Title | Enzyme specificity under dynamic control: a normal mode analysis of alpha-lytic protease. |
| Related PDB | |
| Related UniProtKB | |
| [35] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10500115 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1999 |
| Volume | 96 |
| Pages | 11008-14 |
| Authors | Cunningham EL, Jaswal SS, Sohl JL, Agard DA |
| Title | Kinetic stability as a mechanism for protease longevity. |
| Related PDB | |
| Related UniProtKB | |
| [36] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10802737 |
| Journal | Nat Struct Biol |
| Year | 2000 |
| Volume | 7 |
| Pages | 394-7 |
| Authors | Derman AI, Agard DA |
| Title | Two energetically disparate folding pathways of alpha-lytic protease share a single transition state. |
| Related PDB | |
| Related UniProtKB | |
| [37] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10984533 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 2000 |
| Volume | 97 |
| Pages | 10371-6 |
| Authors | Ash EL, Sudmeier JL, Day RM, Vincent M, Torchilin EV, Haddad KC, Bradshaw EM, Sanford DG, Bachovchin WW |
| Title | Unusual 1H NMR chemical shifts support (His) Cepsilon 1...O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis. |
| Related PDB | |
| Related UniProtKB | |
| [38] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10944390 |
| Journal | Proteins |
| Year | 2000 |
| Volume | 41 |
| Pages | 21-32 |
| Authors | Inuzuka Y, Lazaridis T |
| Title | On the unfolding of alpha-lytic protease and the role of the pro region. |
| Related PDB | |
| Related UniProtKB | |
| [39] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11420442 |
| Journal | Protein Sci |
| Year | 2001 |
| Volume | 10 |
| Pages | 1403-14 |
| Authors | Ota N, Agard DA |
| Title | Enzyme specificity under dynamic control II: Principal component analysis of alpha-lytic protease using global and local solvent boundary conditions. |
| Related PDB | |
| Related UniProtKB | |
| [40] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12102628 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 8860-7 |
| Authors | Cunningham EL, Mau T, Truhlar SM, Agard DA |
| Title | The pro region N-terminal domain provides specific interactions required for catalysis of alpha-lytic protease folding. |
| Related PDB | |
| Related UniProtKB | |
| [41] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11814352 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 1587-90 |
| Authors | Ivanov D, Bachovchin WW, Redfield AG |
| Title | Boron-11 pure quadrupole resonance investigation of peptide boronic acid inhibitors bound to alpha-lytic protease. |
| Related PDB | |
| Related UniProtKB | |
| [42] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11797014 |
| Journal | Nature |
| Year | 2002 |
| Volume | 415 |
| Pages | 343-6 |
| Authors | Jaswal SS, Sohl JL, Davis JH, Agard DA |
| Title | Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. |
| Related PDB | |
| Related UniProtKB | |
| [43] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14609332 |
| Journal | Biochemistry |
| Year | 2003 |
| Volume | 42 |
| Pages | 13212-9 |
| Authors | Cunningham EL, Agard DA |
| Title | Interdependent folding of the N- and C-terminal domains defines the cooperative folding of alpha-lytic protease. |
| Related PDB | |
| Related UniProtKB | |
| [44] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14504841 |
| Journal | Eur Biophys J |
| Year | 2004 |
| Volume | 33 |
| Pages | 83-8 |
| Authors | Cabrita LD, Bottomley SP |
| Title | How do proteins avoid becoming too stable? Biophysical studies into metastable proteins. |
| Related PDB | |
| Related UniProtKB | |
| [45] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15111063 |
| Journal | J Mol Biol |
| Year | 2004 |
| Volume | 338 |
| Pages | 999-1013 |
| Authors | Fuhrmann CN, Kelch BA, Ota N, Agard DA |
| Title | The 0.83 A resolution crystal structure of alpha-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain. |
| Related PDB | |
| Related UniProtKB | |
| [46] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14739318 |
| Journal | Protein Sci |
| Year | 2004 |
| Volume | 13 |
| Pages | 325-31 |
| Authors | Cunningham EL, Agard DA |
| Title | Disabling the folding catalyst is the last critical step in alpha-lytic protease folding. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the peptidase family-S1E.
According to the literature [4] & [37], |
| Created | Updated |
|---|---|
| 2004-11-18 | 2011-02-23 |