| IED ID | IndEnz0015000121 |
| Enzyme Type ID | laccase000121 |
| Protein Name |
Adenosine deaminase RL5 EC 3.5.4.4 Laccase RL5 Multicopper oxidase RL5 Polyphenol oxidase EC 1.10.3.- Purine nucleoside phosphorylase RL5 EC 2.4.2.1 S-methyl-5'-thioadenosine phosphorylase RL5 EC 2.4.2.28 |
| Gene Name | rl5 |
| Organism | Unknown prokaryotic organism |
| Taxonomic Lineage | cellular organisms Bacteria environmental samples Unknown prokaryotic organism |
| Enzyme Sequence | MIELEKLDFAKSVEGVEAFSTTRGQVDGRNAYSGVNLCDYVGDDALRVLDARLTLAMQLGVDLDDLVMPRQTHSCRVAVIDERFRALDIDEQEAALEGVDALVTRLQGIVIGVNTADCVPIVLVDSQAGIVAVSHAGWRGTVGRIAKAVVEEMCRQGATVDRIQAAMGPSICQDCFEVGDEVVEAFKKAHFNLNDIVVRNPATGKAHIDLRAANRAVLVAAGVPAANIVESQHCSRCEHTSFFSARRLGINSGRTFTGIYRK |
| Enzyme Length | 262 |
| Uniprot Accession Number | Q1EIR0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:P84138};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474, ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000250|UniProtKB:P84138};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:P84138};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000250|UniProtKB:P84138};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000250|UniProtKB:P84138}; |
| DNA Binding | |
| EC Number | 3.5.4.4; 1.10.3.-; 2.4.2.1; 2.4.2.28 |
| Enzyme Function | FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine (By similarity). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (By similarity). Also has adenosine deaminase activity (By similarity). Also acts as a multicopper oxidase able to oxidize a wide variety of polyphenols and related compounds in vitro (PubMed:16740638). Displays substrate preference as follows: syringaldazine > 2,6-dimethoxyphenol > veratryl alcohol > guaiacol > tetramethylbenzidine > 4-methoxybenzyl alcohol > 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) >> phenol red > 1-hydroxybenzotriazole (PubMed:16740638). Cannot use 3,4-dimetoxybenzyl alcohol and violuric acid as substrates (PubMed:16740638). As this enzyme is derived from a rumen microbial community, it may have a role in the digestion of complex plant materials such as ryegrass lignin (PubMed:16740638). {ECO:0000250|UniProtKB:P84138, ECO:0000269|PubMed:16740638}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 60 degrees Celsius. Is fully stable at this temperature. {ECO:0000269|PubMed:16740638}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0-5.0. Activity is very high over a broad pH range from 4.0 to 9.0. Exhibits more than 70% activity at pH 3.5 and 9.5. {ECO:0000269|PubMed:16740638}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (12); Mutagenesis (16) |
| Keywords | Copper;Hydrolase;Metal-binding;Oxidoreductase;Transferase;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,282 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; KM=0.43 uM for syringaldazine (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; KM=0.45 uM for 2,6-dimethoxyphenol (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; Note=kcat is 18 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid as substrate. kcat is 660 sec(-1) with syringaldazine as substrate. kcat is 1175 sec(-1) with 2,6-dimethoxyphenol as substrate (at pH 4.5 and 40 degrees Celsius). {ECO:0000269|PubMed:16740638}; |
| Metal Binding | METAL 36; /note=Copper 3; /evidence=ECO:0000305|PubMed:16740638; METAL 40; /note=Copper 3; /evidence=ECO:0000305|PubMed:16740638; METAL 68; /note=Copper 3; /evidence=ECO:0000305|PubMed:16740638; METAL 73; /note=Copper 1; catalytic; /evidence=ECO:0000305|PubMed:16740638; METAL 75; /note=Copper 1; /evidence=ECO:0000305|PubMed:16740638; METAL 114; /note=Copper 3; /evidence=ECO:0000305|PubMed:16740638; METAL 118; /note=Copper 1; catalytic; /evidence=ECO:0000305|PubMed:16740638; METAL 135; /note=Copper 1; catalytic; /evidence=ECO:0000305|PubMed:16740638; METAL 172; /note=Copper 2; /evidence=ECO:0000305|PubMed:16740638; METAL 175; /note=Copper 2; /evidence=ECO:0000305|PubMed:16740638; METAL 234; /note=Copper 2; /evidence=ECO:0000305|PubMed:16740638; METAL 237; /note=Copper 2; /evidence=ECO:0000305|PubMed:16740638 |
| Rhea ID | RHEA:27642; RHEA:27643; RHEA:11852; RHEA:11853; RHEA:27646; RHEA:27647; RHEA:24408; RHEA:24409 |
| Cross Reference Brenda |