1.1.1.431: D-xylose reductase (NADPH)
This is an abbreviated version!
For detailed information about D-xylose reductase (NADPH), go to the full flat file.
Reaction
Synonyms
ALR1, Cb-XR, CbXR, CtXR, D-xylose reductase, D-xylose reductase 1, D-xylose reductase 2, D-xylose reductase 3, DnXR, GRE3, monospecific xylose reductase, More, msXR, NAD(P)H-dependent D-xylose reductase, NAD(P)H-dependent xylose reductase, NADPH dependent D-xylose reductase, NADPH-dependent D-xylose reductase II,III, NADPH-dependent xylose reductase, NADPH-preferring xylose reductase, NRRL3_10868, SsXR, Texr, TrxR, XR1, XR2, XR3, XRTL, XYL1, xylose reductase, xyr8, XyrA, XyrB
ECTree
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Subunits
Subunits on EC 1.1.1.431 - D-xylose reductase (NADPH)
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dimer
homodimer
monomer
monomer or dimer
additional information
x * 39200, recombinant enzyme, SDS-PAGE, x * 36740, sequence calculation
monomer
-
x * 39200, recombinant enzyme, SDS-PAGE, x * 36740, sequence calculation
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
additional information
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
additional information
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
-
additional information
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
-
additional information
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
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