| IED ID | IndEnz0002014282 |
| Enzyme Type ID | protease014282 |
| Protein Name |
Deglycase PfpI EC 3.5.1.124 Intracellular protease I EC 3.4.22.- |
| Gene Name | pfpI PF1719 |
| Organism | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus furiosus Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Enzyme Sequence | MKILFLSANEFEDVELIYPYHRLKEEGHEVYIASFEKGVITGKHGYSVKVDLTFDEVNPDEFDALVLPGGRAPERVRLNEKAVEIARKMFTEGKPVATICHGPQILISAGVLKGRKGTSYIGIRDDMINAGVEWIDREVVVDGNWVSSRHPGDLYAWMREFVKLLK |
| Enzyme Length | 166 |
| Uniprot Accession Number | Q51732 |
| Absorption | |
| Active Site | ACT_SITE 100; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU00608; ACT_SITE 101; /evidence=ECO:0000255|PROSITE-ProRule:PRU00608 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}; |
| DNA Binding | |
| EC Number | 3.5.1.124; 3.4.22.- |
| Enzyme Function | FUNCTION: Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals (Probable). Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively (PubMed:27530919). Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals (By similarity). Thus, was shown to afford full protection against glycation of thioredoxin by glyoxal (PubMed:27530919). Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (By similarity). Prevents acrylamide formation in asparagine/glyoxal and asparagine/sugar mixtures, likely by degrading asparagine/glyoxal Maillard adducts formed at high temperatures (PubMed:27530919). Also displays proteolytic activity (PubMed:8626329, PubMed:16535492). Cleaves at the carboxyl side of both basic and hydrophobic residues in the P1 position, indicating trypsin- and chymotrypsin-like specificities (PubMed:16535492). {ECO:0000250|UniProtKB:P45470, ECO:0000269|PubMed:16535492, ECO:0000269|PubMed:27530919, ECO:0000269|PubMed:8626329}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 84-97 degrees Celsius for proteolytic activity (PubMed:8626329, PubMed:16535492). Thermostable. Displays a half-life of 19 minutes at 95 degrees Celsius (PubMed:8626329). {ECO:0000269|PubMed:16535492, ECO:0000269|PubMed:8626329}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.3 for proteolytic activity with AAF-MCA as substrate. {ECO:0000269|PubMed:16535492}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1) |
| Keywords | Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8626329}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,791 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:49548; RHEA:49552; RHEA:49556; RHEA:57188; RHEA:57192; RHEA:57196 |
| Cross Reference Brenda | 3.4.22.B20;3.5.1.124;4.2.1.130; |