Detail Information for IndEnz0019000037
IED ID IndEnz0019000037
Enzyme Type ID polyphenol oxidase000037
Protein Name Purine nucleoside phosphorylase BT_4389
EC 2.4.2.1
Adenosine deaminase BT_4389
EC 3.5.4.4
S-methyl-5'-thioadenosine phosphorylase BT_4389
EC 2.4.2.28
Gene Name BT_4389
Organism Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Taxonomic Lineage cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Bacteroidaceae Bacteroides Bacteroides thetaiotaomicron Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Enzyme Sequence MISITKDKRMLGYESLSSYSNISHFVTTRQGGCSEGNYASFNCTPYSGDEAEKVRRNQTLLMEGMSQIPEELVIPVQTHETNYLLIGDAYLSASSQQRQEMLHGVDALITREPGYCLCISTADCVPVLVYDKKHGAIAAIHAGWRGTVAYIVRDTLLRMEKEFGTSGEDVVACIGPSISLASFEVGEEVYEAFQKNGFDMPRISIRKEETGKHHIDLWEANRMQILAFGVPSGQVELARICTYIHHDEFFSARRLGIKSGRILSGIMIHK
Enzyme Length 270
Uniprot Accession Number Q89ZI8
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 2.4.2.1; 3.5.4.4; 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. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity. {ECO:0000250|UniProtKB:P84138}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 52 degrees Celsius. Maintains more than 80% activity at 55 degrees Celsius. {ECO:0000269|PubMed:16740638};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-6.0. Maintains 80% activity at pH 4.0-7.5. {ECO:0000269|PubMed:16740638};
Pathway
nucleotide Binding
Features Chain (1); Metal binding (3)
Keywords Copper;Hydrolase;Metal-binding;Oxidoreductase;Reference proteome;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 30,118
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.0 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; KM=0.83 uM for syringaldazine (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; Note=kcat is 13000 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid as substrate. kcat is 33300 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius). {ECO:0000269|PubMed:16740638};
Metal Binding METAL 79; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 124; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 141; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138
Rhea ID RHEA:27642; RHEA:27643; RHEA:11852; RHEA:11853; RHEA:27646; RHEA:27647; RHEA:24408; RHEA:24409
Cross Reference Brenda