| IED ID | IndEnz0004000039 |
| Enzyme Type ID | xylanase000039 |
| Protein Name |
4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic EC 3.2.1.182 Beta-D-glucoside glucohydrolase Beta-glucosidase 1 ZmGlu1 EC 3.2.1.21 |
| Gene Name | GLU1 |
| Organism | Zea mays (Maize) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae PACMAD clade Panicoideae Andropogonodae Andropogoneae Tripsacinae Zea Zea mays (Maize) |
| Enzyme Sequence | MAPLLAAAMNHAAAHPGLRSHLVGPNNESFSRHHLPSSSPQSSKRRCNLSFTTRSARVGSQNGVQMLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGESNWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMGMDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLENGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYFAKVCFDNFGDKVKNWLTFNEPQTFTSFSYGTGVFAPGRCSPGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKRDDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLEPVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLNYYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIGPPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGDVDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNVQGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKESAKWLKEFNTAKKPSKKILTPA |
| Enzyme Length | 566 |
| Uniprot Accession Number | P49235 |
| Absorption | |
| Active Site | ACT_SITE 245; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q7XKV4; ACT_SITE 460; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q7XKV4 |
| Activity Regulation | ACTIVITY REGULATION: Reversibly inhibited by micromolar concentrations of Hg(2+) or Ag(+), but irreversibly inhibited by alkylation in presence of urea. Competitive inhibition by p-nitrophenyl beta-D-thioglucoside (pNPTGlc), glucotetrazole, and para-hydroxy-S-mandelonitrile beta-glucoside (dhurrin). {ECO:0000269|PubMed:11106394, ECO:0000269|PubMed:11171077}. |
| Binding Site | BINDING 92; /note="Substrate"; /evidence="ECO:0000269|PubMed:11106394, ECO:0000269|PubMed:12684498, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49"; BINDING 196; /note="Substrate"; /evidence="ECO:0000269|PubMed:11106394, ECO:0007744|PDB:1E56"; BINDING 244; /note="Substrate"; /evidence="ECO:0000269|PubMed:11106394, ECO:0007744|PDB:1E56"; BINDING 387; /note="Substrate"; /evidence="ECO:0000269|PubMed:11106394, ECO:0007744|PDB:1E56"; BINDING 511; /note="Substrate"; /evidence="ECO:0000269|PubMed:11106394, ECO:0000269|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49"; BINDING 527; /note="Substrate"; /evidence="ECO:0000269|PubMed:11106394, ECO:0007744|PDB:1E56" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; CATALYTIC ACTIVITY: Reaction=DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA; Xref=Rhea:RHEA:33975, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:18048, ChEBI:CHEBI:37573; EC=3.2.1.182; CATALYTIC ACTIVITY: Reaction=DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA; Xref=Rhea:RHEA:33979, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:63558, ChEBI:CHEBI:63670; EC=3.2.1.182; |
| DNA Binding | |
| EC Number | 3.2.1.182; 3.2.1.21 |
| Enzyme Function | FUNCTION: Is implicated in many functions such as ABA metabolism, hydrolysis of conjugated gibberellins, conversion of storage forms of cytokinins to active forms. Also acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth. The preferred substrate is DIMBOA-beta-D-glucoside. Hydrolyzes the chromogenic substrate 6-bromo-2-naphthyl-beta-D-glucoside (6BNGlc) and various artificial aryl beta-glucosides. No activity with cellobiose, arbutin, gentiobiose, linamarin or dhurrin as substrates. {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Loses activity when is heated at 55 degrees Celsius. {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.8. {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (16); Binding site (6); Chain (1); Compositional bias (1); Disulfide bond (1); Helix (25); Mutagenesis (8); Region (5); Sequence conflict (3); Transit peptide (1); Turn (4) |
| Keywords | 3D-structure;Chloroplast;Cytokinin signaling pathway;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Plastid;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1E1E; 1E1F; 1E4L; 1E4N; 1E55; 1E56; 1H49; 1HXJ; 1V08; |
| Mapped Pubmed ID | 19227973; 19712949; 9796109; |
| Motif | |
| Gene Encoded By | |
| Mass | 64,237 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mM for 4-methylumbelliferyl beta-D-glucopyranoside (MUG) {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=0.64 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=0.41 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme) {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=98 uM for DIMBOA-beta-D-glucoside {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=0.251 mM for n-octyl-beta-D-glucopyranoside {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=0.394 mM for p-nitrophenyl beta-D-xyloside {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=0.648 mM for p-nitrophenyl beta-D-fucopyranoside {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=0.674 mM for p-nitrophenyl beta-D-cellobioside {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=0.769 mM for p-nitrophenyl beta-D-mannopyranoside {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=1.64 mM for o-nitrophenyl beta-D-glucopyranoside {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=1.42 mM for o-nitrophenyl beta-D-glucopyranoside (with recombinant enzyme) {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; KM=4.32 mM for p-nitrophenyl beta-D-galactopyranoside {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; Vmax=225.4 umol/h/ug enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme) {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; Vmax=282.7 umol/h/ug enzyme with o-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme) {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5}; |
| Metal Binding | |
| Rhea ID | RHEA:33975; RHEA:33979 |
| Cross Reference Brenda | 3.2.1.182;3.2.1.21; |