| IED ID | IndEnz0008000449 |
| Enzyme Type ID | cellulase000449 |
| Protein Name |
NAD P H-dependent D-xylose reductase xyl1 XR EC 1.1.1.- |
| Gene Name | xyl1 |
| Organism | Hypocrea jecorina (Trichoderma reesei) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei) |
| Enzyme Sequence | MASPTLKLNSGYDMPQVGFGLWKVDNAVCADTVYNAIKAGYRLFDGACDYGNEKECGEGVARAIKDGLVKREDLFIVSKLWQTFHDEDKVEPITRRQLADWQIDYFDLFLVHFPAALEYVDPSVRYPPGWFYDGKSEVRWSKTTTLQQTWGAMERLVDKGLARSIGVSNYQAQSVYDALIYARIKPATLQIEHHPYLQQPDLVSLAQTEGIVVTAYSSFGPTGFMELDMPRAKSVAPLMDSPVIKALADKHRRTPAQVLLRWATQRGIAVIPKTSRPEVMAQNLDNTSFDLDSEDLAKIADMDLNIRFNKPTNYFSANKLYLFG |
| Enzyme Length | 324 |
| Uniprot Accession Number | Q876L8 |
| Absorption | |
| Active Site | ACT_SITE 50; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 112; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an alditol + NAD(+) = an aldose + H(+) + NADH; Xref=Rhea:RHEA:12785, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555, ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:17924946}; CATALYTIC ACTIVITY: Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH; Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555, ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:17924946}; CATALYTIC ACTIVITY: Reaction=NAD(+) + xylitol = D-xylose + H(+) + NADH; Xref=Rhea:RHEA:27441, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151, ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:17924946}; CATALYTIC ACTIVITY: Reaction=NADP(+) + xylitol = D-xylose + H(+) + NADPH; Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151, ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:17924946}; |
| DNA Binding | |
| EC Number | 1.1.1.- |
| Enzyme Function | FUNCTION: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway. Also major aldose reductase in pentose and D-galactose catabolism. Reduces the pentose L-arabinose and the hexose D-galactose to their respective polyols. Responsible for extracellular beta-galactosidase formation and cellulase induction during growth on lactose. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Carbohydrate metabolism; D-xylose degradation.; PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route): step 1/5. |
| nucleotide Binding | NP_BIND 168..169; /note=NAD; /evidence=ECO:0000250; NP_BIND 217..226; /note=NAD; /evidence=ECO:0000250; NP_BIND 273..283; /note=NAD; /evidence=ECO:0000250 |
| Features | Active site (1); Binding site (1); Chain (1); Nucleotide binding (3); Site (1) |
| Keywords | Carbohydrate metabolism;NAD;NADP;Oxidoreductase;Xylose metabolism |
| Interact With | |
| Induction | INDUCTION: Regulated by carbon source. Most abundant during growth on D-xylose and L-arabinose. {ECO:0000269|PubMed:17924946}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 36,565 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 mM for D-xylose {ECO:0000269|PubMed:17924946}; KM=24 mM for D-ribose {ECO:0000269|PubMed:17924946}; KM=41 mM for L-arabinose {ECO:0000269|PubMed:17924946}; KM=82 mM for D-galactose {ECO:0000269|PubMed:17924946}; KM=366 mM for D-glucose {ECO:0000269|PubMed:17924946}; KM=11 mM for xylitol {ECO:0000269|PubMed:17924946}; KM=76 mM for L-arabinitol {ECO:0000269|PubMed:17924946}; KM=155 mM for galactitol {ECO:0000269|PubMed:17924946}; KM=98 mM for ribitol {ECO:0000269|PubMed:17924946}; KM=159 mM for D-sorbitol {ECO:0000269|PubMed:17924946}; KM=0.023 mM for NADPH {ECO:0000269|PubMed:17924946}; KM=0.26 mM for NADH {ECO:0000269|PubMed:17924946}; Vmax=176 nmol/sec/mg enzyme toward NADPH {ECO:0000269|PubMed:17924946}; Vmax=0.42 nmol/sec/mg enzyme toward NADH {ECO:0000269|PubMed:17924946}; Vmax=225 nmol/sec/mg enzyme with D-xylose as substrate for the reverse reaction {ECO:0000269|PubMed:17924946}; Vmax=9 nmol/sec/mg enzyme with xylitol as substrate for the forward reaction {ECO:0000269|PubMed:17924946}; Vmax=125 nmol/sec/mg enzyme with ribose as substrate for the reverse reaction {ECO:0000269|PubMed:17924946}; Vmax=9 nmol/sec/mg enzyme with ribitol as substrate for the forward reaction {ECO:0000269|PubMed:17924946}; Vmax=175 nmol/sec/mg enzyme with L-arabinose as substrate for the reverse reaction {ECO:0000269|PubMed:17924946}; Vmax=16 nmol/sec/mg enzyme with L-arabinitol as substrate for the forward reaction {ECO:0000269|PubMed:17924946}; Vmax=18 nmol/sec/mg enzyme with D-galactose as substrate for the reverse reaction {ECO:0000269|PubMed:17924946}; Vmax=9 nmol/sec/mg enzyme with galactitol as substrate for the forward reaction {ECO:0000269|PubMed:17924946}; Vmax=66 nmol/sec/mg enzyme with D-glucose as substrate for the reverse reaction {ECO:0000269|PubMed:17924946}; Vmax=18 nmol/sec/mg enzyme with D-sorbitol as substrate for the forward reaction {ECO:0000269|PubMed:17924946}; |
| Metal Binding | |
| Rhea ID | RHEA:12785; RHEA:12789; RHEA:27441; RHEA:27445 |
| Cross Reference Brenda | 1.1.1.307; |