Type | Count |
---|---|
Connectase | 2 |
Intein | 5 |
PAL | 21 |
PBP-like cyclase | 1 |
POP-like cyclase | 3 |
Sortase | 5 |
Subtiligase | 3 |
Subtilisin-like ligase | 1 |
Trypsiligase | 1 |
No description available.
Inteins are naturally occurring self-splicing enzymes that excise themselves from a precursor protein while simultaneously ligating the remaining protein fragments, known as exteins. Inteins have garnered significant interest in the development of controllable protein assembly systems, protein purification methods, and tools for controlling gene expression. Engineering of inteins have focused on splicing efficiency and specificity, conditional splicing, minimization/splitting, and stability.
Peptide asparaginyl ligases (PALs) are cysteine proteases from C13 family that catalyze peptide cyclization.The includes vacuolar processing enzymes involved in protein maturation.
Name | Host Organism | Catalytic residues | Details |
---|---|---|---|
Butelase-1 | Clitoria ternatea | H165-C207 | View |
OaAEP1b | Oldenlandia affinis | H175-C217 | View |
OaAEP3 | Oldenlandia affinis | - | View |
OaAEP4 | Oldenlandia affinis | - | View |
OaAEP5 | Oldenlandia affinis | - | View |
VyPAL2 | Viola yedoensis | H172-C214 | View |
VyPAL2-I244V | Viola yedoensis | H172-C215 | View |
VaPAL1 | Viola albida | - | View |
VaPAL2 | Viola albida | - | View |
VvPAL1 | Viola verecunda | - | View |
VvPAL2 | Viola verecunda | - | View |
VoPAL1 | Viola orientalis | - | View |
VuPAL1 | Viola uliginosa | - | View |
HaPAL1 | Helianthus annuus | - | View |
VyPAL1 | Viola yedoensis | - | View |
VyPAL4 | Viola yedoensis | - | View |
VyPAL5 | Viola yedoensis | - | View |
VbAEP1 | Viola betonicifolia | - | View |
HeAEP3 | Hybanthus enneaspermus | - | View |
Vc1c | Viola canadensis | - | View |
ConPAL3 | Artificial | - | View |
Penicillin-binding protein (PBP)-like cyclase involved in the final step of macrocyclization in some NRPs. They act like transestrase (TE) domain of the NRPS complex but physically discrete from the megasynthetase, such as SurE in surugamide biosynthesis.
Name | Host Organism | Catalytic residues | Details |
---|---|---|---|
SurE | - | - | View |
Propyl oligopeptidase
Sortases are Cys transpeptidases found in Gram-positive bacteria, essential for anchoring virulence-associated surface proteins to the cell wall. They specifically recognize pentapeptide signals, such as LPXTG for SrtA, and catalyze peptide bond formation between the conserved Thr and the N-terminal Gly of peptidoglycan precursors. The enzymatic versatility of sortases, particularly SrtA, has been harnessed for a broad range of biotechnological applications. Recent engineering efforts have focused on enhancing the specificity, efficiency, and stability of sortase enzymes.
Subtiligases are engineered ligase variants derived from the subtilisin family of proteases. They function by ligating a peptide ester to the N-terminal α-amine of a protein or peptide, providing irreversible reactions and broader sequence tolerance compared to other transpeptidase-type ligation enzymes. Engineered versions of subtiligase have achieved better ligation/hydrolysis ratio, high tolerance to organic solvents, and tailored specificity, enhancing their utility in protein engineering and biochemical applications.
No description available.
Name | Host Organism | Catalytic residues | Details |
---|---|---|---|
PatG | Prochloron didemni | H68-D648-S783 | View |
No description available.
Name | Host Organism | Catalytic residues | Details |
---|---|---|---|
Trypsiligase | - | - | View |