Detail Information for IndEnz0004000039
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;