Catalytic mechanism and substrate selectivity of aldo-keto reductases: Insights from structure-function studies of Candida tenuis xylose reductase
Open accessAbstract
Aldo-keto reductases (AKRs) constitute a large protein superfamily of mainly NAD(P)-dependent oxidoreductases involved in carbonyl metabolism. Catalysis is promoted by a conserved tetrad of active site residues (Tyr, Lys, Asp and His). Recent results of structure-function relationship studies for xylose reductase (AKR2B5) require an update of the proposed catalytic mechanism. Electrostatic stabilization by the epsilon-NH3+ group of Lys is a key source of catalytic power of xylose reductase. A molecular-level analysis of the substrate binding pocket of xylose reductase provides a case of how a very broadly specific AKR achieves the requisite selectivity for its physiological substrate and could serve as the basis for the design of novel reductases with improved specificities for biocatalytic applications.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
AKR catalytic mechanism is similar to that of SDRs, using an active-site Tyr and an assisting Lys to deprotonate the Tyr hydroxyl.
“The catalytic mechanism of AKR’s, in principle, is similar to that found in SDR’s with an active site Tyr residue and an assisting Lys residue facilitating the deprotonation of the Tyr hydroxyl group.384”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [384]
The Acid/base Catalysis—Tyr-51 section identifies an active-site Tyr as the likely catalytic acid. But it says that, in AKR2B5, interaction with Lys-80 is not required to lower Tyr-51’s pKa; the Electrostatic stabilization—Lys-80 section instead proposes an electrostatic role for Lys. The cited passages do not establish the stated comparison with SDRs. Page numbers are unavailable in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Comparative anatomy of the aldo–keto reductase superfamily
Jez, J. M., BENNETT, M. J., Schlegel, B. P., Lewis, M., & Penning, T. M. (1997) · Biochemical Journal · doi:10.1042/bj3260625 · Cited by 603 · see citing works
The Aldo-Keto Reductase Superfamily
Bohren, K. M., Bullock, B., Wermuth, B., & Gabbay, K. H. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60566-6 · Cited by 453 · see citing works
Wilson, D. K., Bohren, K. M., Gabbay, K. H., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1621098 · Cited by 434 · see citing works
Self-citationThe aldo-keto reductase superfamily homepage
Hyndman, D., Bauman, D. R., Heredia, V. V., & Penning, T. M. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00193-x · Cited by 317 · see citing works
Structure of a voltage-dependent K+ channel β subunit
Gulbis, J. M., Mann, S., & MacKinnon, R. (1999) · Cell · doi:10.1016/s0092-8674(00)80805-3 · Cited by 283 · see citing works
The role of redox balances in the anaerobic fermentation of xylose by yeasts
Bruinenberg, P. M., de Bot, P. H. M., van Dijken, J. P., & Scheffers, W. A. (1983) · Applied Microbiology and Biotechnology · doi:10.1007/bf00500493 · Cited by 264 · see citing works
Metabolic Engineering of Saccharomyces cerevisiae for Xylose Utilization
Hahn‐Hägerdal, B., Wahlbom, C. F., Gárdonyi, M., van Zyl, W. H., Otero, R. R. C., & Jönsson, L. J. (2001) · Advances in biochemical engineering, biotechnology · doi:10.1007/3-540-45300-8_4 · Cited by 226 · see citing works
Novel bioreduction system for the production of chiral alcohols
Kataoka, M., Kita, K., Wada, M., Yasohara, Y., Hasegawa, J., & Shimizu, S. (2003) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-003-1347-y · Cited by 207 · see citing works
Aldose reductase and ϱ‐crystallin belong to the same protein superfamily as aldehyde reductase
Carper, D. A., Nishimura, C., Shinohara, T., Dietzchold, B., Wistow, G. J., Craft, C. M., Kador, P. F., & Kinoshita, J. H. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80905-5 · Cited by 171 · see citing works
Bohren, K. M., Grimshaw, C. E., Lai, C.-J., Harrison, D. H. T., Ringe, D., Petsko, G. A., & Gabbay, K. H. (1994) · Biochemistry · doi:10.1021/bi00174a007 · Cited by 171 · see citing works
Pettersson, G. (1987) · PubMed · Cited by 166 · see citing works
KONDO, K., KAI, M., SETOGUCHI, Y., EGGERTSEN, G., SJÖBLOM, P., SETOGUCHI, T., OKUDA, K., & BJÖRKHEM, I. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19947.x · Cited by 139 · see citing works
Schlegel, B. P., Jez, J. M., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi9723055 · Cited by 139 · see citing works
Petschacher, B., Leitgeb, S., Kavanagh, K. L., Wilson, D. K., & Nidetzky, B. (2004) · Biochemical Journal · doi:10.1042/bj20040363 · Cited by 123 · see citing works
Self-citationMechanism of Human Aldehyde Reductase: Characterization of the Active Site Pocket
Barski, O. A., Gabbay, K. H., Grimshaw, C. E., & Bohren, K. M. (1995) · Biochemistry · doi:10.1021/bi00035a036 · Cited by 120 · see citing works
Aldose reductase structures: implications for mechanism and inhibition
El-Kabbani, O. A. L., Ruiz, F. M., Darmanin, C., & Chung, R. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3403-2 · Cited by 116 · see citing works
Microbial aldo-keto reductases
Ellis, E. M. (2002) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2002.tb11425.x · Cited by 113 · see citing works
Modulation of Voltage-dependent Shaker Family Potassium Channels by an Aldo-Keto Reductase*
Weng, J., Cao, Y., Moss, N., & Zhou, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513809200 · Cited by 112 · see citing works
Neuhauser, W., Haltrich, D., Kulbe, K. D., & Nidetzky, B. (1997) · Biochemical Journal · doi:10.1042/bj3260683 · Cited by 108 · see citing works
Self-citationKavanagh, K. L., Klimacek, M., Nidetzky, B., & Wilson, D. K. (2002) · Biochemistry · doi:10.1021/bi025786n · Cited by 104 · see citing works
Self-citationKavanagh, K. L., Klimacek, M., Nidetzky, B., & Wilson, D. K. (2003) · Biochemical Journal · doi:10.1042/bj20030286 · Cited by 70 · see citing works
Self-citationEngineering Steroid 5β-Reductase Activity into Rat Liver 3α-Hydroxysteroid Dehydrogenase
Jez, J. M., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi980294p · Cited by 63 · see citing works
Penning, T. M. (1999) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(99)00038-2 · Cited by 63 · see citing works
The C-Terminal Loop of Aldehyde Reductase Determines the Substrate and Inhibitor Specificity
Barski, O. A., Gabbay, K. H., & Bohren, K. M. (1996) · Biochemistry · doi:10.1021/bi9619740 · Cited by 63 · see citing works
Computer Simulation Studies of the Catalytic Mechanism of Human Aldose Reductase
Várnai, P., & Warshel, A. (2000) · Journal of the American Chemical Society · doi:10.1021/ja994246j · Cited by 62 · see citing works
Structure and function of 3α-hydroxysteroid dehydrogenase
Penning, T. M., Bennett, M. J., Hoog, S. S., Schlegel, B. P., Jez, J. M., & Lewis, M. (1997) · Steroids · doi:10.1016/s0039-128x(96)00167-5 · Cited by 62 · see citing works
Grimshaw, C. E., Bohren, K. M., Lai, C.-J., & Gabbay, K. H. (1995) · Biochemistry · doi:10.1021/bi00044a014 · Cited by 52 · see citing works
Participation of Histidine-51 in Catalysis by Horse Liver Alcohol Dehydrogenase,
LeBrun, L. A., Park, D.-H., Ramaswamy, S., & Plapp, B. V. (2004) · Biochemistry · doi:10.1021/bi036103m · Cited by 52 · see citing works
Ma, H., & Penning, T. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11161 · Cited by 52 · see citing works
Nidetzky, B., Klimacek, M., & Mayr, P. (2001) · Biochemistry · doi:10.1021/bi010148a · Cited by 47 · see citing works
Self-citationSchlegel, B. P., Ratnam, K., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi980475r · Cited by 45 · see citing works
Kratzer, R., Leitgeb, S., Wilson, D. K., & Nidetzky, B. (2005) · Biochemical Journal · doi:10.1042/bj20050831 · Cited by 37 · see citing works
Self-citationNoncovalent Enzyme−Substrate Interactions in the Catalytic Mechanism of Yeast Aldose Reductase
Neuhauser, W., Haltrich, D., Kulbe, K. D., & Nidetzky, B. (1998) · Biochemistry · doi:10.1021/bi9717800 · Cited by 32 · see citing works
Self-citationMayr, P., & Nidetzky, B. (2002) · Biochemical Journal · doi:10.1042/bj20020080 · Cited by 30 · see citing works
Self-citationHeredia, V. V., & Penning, T. M. (2004) · Biochemistry · doi:10.1021/bi0489762 · Cited by 27 · see citing works
Kratzer, R., Kavanagh, K. L., Wilson, D. K., & Nidetzky, B. (2004) · Biochemistry · doi:10.1021/bi035833r · Cited by 25 · see citing works
Self-citationKubata, B. K., Tsuyoshi Inoue, A., Okano, Y., Kabututu, Z. P., Martin, S. K., Lazarus, M., Duszenko, M., Sumii, Y., Kusakari, Y., Matsumura, H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413884200 · Cited by 23 · see citing works
Klimacek, M., Szekely, M., Grießler, R., & Nidetzky, B. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02609-6 · Cited by 20 · see citing works
Self-citationYokochi, N., Yoshikane, Y., Trongpanich, Y., Ohnishi, K., & Yagi, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405344200 · Cited by 19 · see citing works
Heredia, V. V., Cooper, W. C., Kruger, R. G., Jin, Y., & Penning, T. M. (2004) · Biochemistry · doi:10.1021/bi0499563 · Cited by 19 · see citing works
Kratzer, R., & Nidetzky, B. (2005) · Biochemical Journal · doi:10.1042/bj20050167 · Cited by 15 · see citing works
Self-citation
Flagged first, then by citations
4 of the 45 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Kratzer, R., and Nidetzky, B. (2006) Structure-function relationships for Candida tenuis xylose reductase (AKR2B5): properties of H113E mutant. In Enzymology and Molecular Biology of Carbonyl Metabolism-12 (Weiner H., Plapp B., Lindahl, R., and Maser E. eds.). pp. 404 -412, Purdue University Press, West Lafayette, Indiana.
Cited by
Sorted by citations
Chemistry of the Retinoid (Visual) Cycle
Kiser, P. D., Golczak, M., & Palczewski, K. (2014) · Chemical Reviews · doi:10.1021/cr400107q · Cited by 353 · see citing works
Laskar, A. A., & Younus, H. (2018) · Drug Metabolism Reviews · doi:10.1080/03602532.2018.1555587 · Cited by 202 · see citing works
Enzymes for Detoxification of Various Mycotoxins: Origins and Mechanisms of Catalytic Action
Lyagin, I., & Efremenko, E. N. (2019) · Molecules · doi:10.3390/molecules24132362 · Cited by 185 · see citing works
Simpson, P. J., Tantitadapitak, C., Reed, A. M., Mather, O. C., Bunce, C. M., White, S. A., & Ride, J. P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.023 · Cited by 161 · see citing works
Kawai, M., Furuta, Y., Yahara, K., Tsuru, T., Oshima, K., Handa, N., Takahashi, N. K., Yoshida, M., Azuma, T., Hattori, M., et al. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-104 · Cited by 152 · see citing works
Computational design of Candida boidinii xylose reductase for altered cofactor specificity
Khoury, G. A., Fazelinia, H., Chin, J. W., Pantazes, R. J., Cirino, P. C., & Maranas, C. D. (2009) · Protein Science · doi:10.1002/pro.227 · Cited by 91 · see citing works
Campbell, E., Wheeldon, I. R., & Banta, S. A. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22869 · Cited by 60 · see citing works
Han, Y., Bai, W., Ding, C. X., Liang, J., Wu, S., & Tan, R. X. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c05421 · Cited by 52 · see citing works
Wang, H., He, Z., Luo, L., Zhao, X., Lu, Z., Luo, T., Li, M., & Zhang, Y. (2018) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2018.01.001 · Cited by 38 · see citing works
Luo, X., Wang, Y., & Zheng, Y. (2015) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2015.06.004 · Cited by 34 · see citing works
Amaya, I., Osorio, S., Martínez-Ferri, E., Lima‐Silva, V., Doblas, V. G., Fernández-Muñoz, R., Fernie, A. R., Botella, M. A., & Valpuesta, V. (2014) · Biotechnology Journal · doi:10.1002/biot.201400279 · Cited by 34 · see citing works
Wang, Y., Liu, X., Luo, X., Liu, Z., & Zheng, Y. (2015) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2015.08.018 · Cited by 28 · see citing works
Contente, M. L., Serra, I., Palazzolo, L., Parravicini, C., Gianazza, E., Eberini, I., Pinto, A., Guidi, B., Molinari, F., & Romano, D. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00047a · Cited by 28 · see citing works
Artificial Intelligence-Driven de Novo Design of Robust Enzymes to Enhance Their Performance
Tang, M., Ge, F., Li, A., Hu, L., Wang, C., Tang, J., Song, X., Liu, X., Shi, H. S., & Tan, Z. (2025) · ACS Synthetic Biology · doi:10.1021/acssynbio.5c00452 · Cited by 28 · see citing works
Cervera, E. C., Porté, S., Fernández, M. R., Farrés, J., Parés, X., & Biosca, J. A. (2013) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.12.006 · Cited by 25 · see citing works
Chu, X., He, S., Liu, Y., Liu, Y., Feng, F., Guo, Q., Zhao, L., & Sun, H. (2021) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2021.109746 · Cited by 26 · see citing works
Kumar, S., & Gummadi, S. N. (2011) · Bioresource Technology · doi:10.1016/j.biortech.2011.07.030 · Cited by 24 · see citing works
Wang, Z., Zhou, S., Zhang, S., Zhang, S., Zhu, F., Jin, X., Chen, Z., & Xu, X. (2017) · Scientific Reports · doi:10.1038/s41598-017-03947-8 · Cited by 24 · see citing works
Lugani, Y., Puri, M., & Sooch, B. S. (2021) · European Food Research and Technology · doi:10.1007/s00217-020-03674-x · Cited by 23 · see citing works
Cheng, P., Wang, J., Wu, Y., Jiang, X., Pei, X., & Su, W. (2019) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2019.04.001 · Cited by 23 · see citing works
Klaubauf, S., Ribot, C., Melayah, D., Lagorce, A., Lebrun, M., & de Vries, R. P. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.03.003 · Cited by 20 · see citing works
Zhang, M., Puri, A. K., Wang, Z., Singh, S., & Permaul, K. (2019) · Bioresource Technology · doi:10.1016/j.biortech.2019.02.102 · Cited by 20 · see citing works
Xylitol Production by Candida Species from Hydrolysates of Agricultural Residues and Grasses
West, T. P. (2021) · Fermentation · doi:10.3390/fermentation7040243 · Cited by 18 · see citing works
Wang, J., Cheng, P., Wu, Y., Wang, A., Liu, F., & Pei, X. (2018) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2018.12.011 · Cited by 18 · see citing works
Dasgupta, D., Ghosh, D., Bandhu, S., Agrawal, D., Suman, S. K., & Adhikari, D. K. (2015) · Process Biochemistry · doi:10.1016/j.procbio.2015.11.007 · Cited by 17 · see citing works
Co-Factor Binding Confers Substrate Specificity to Xylose Reductase from Debaryomyces hansenii
Biswas, D., Pandya, V. K., Singh, A. K., Mondal, A. K., & Kumaran, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045525 · Cited by 17 · see citing works
Paidimuddala, B., Mohapatra, S. B., Gummadi, S. N., & Manoj, N. (2018) · FEBS Journal · doi:10.1111/febs.14667 · Cited by 17 · see citing works
Komeda, H., Yamasaki-Yashiki, S., Hoshino, K., & Asano, Y. (2014) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2014.06.012 · Cited by 16 · see citing works
Zhang, L., Sun, Z., Xu, G., & Ni, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.132238 · Cited by 14 · see citing works
Yadav, R., & Prasad, R. (2014) · Planta · doi:10.1007/s00425-014-2076-4 · Cited by 14 · see citing works
Zhang, W., Zhu, T., Li, H., Qin, F., Zhang, F., Zhang, R., Jia, X., Qin, B. Y., & You, S. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-09932-7 · Cited by 14 · see citing works
Wu, X., Zhang, C., Xing, X., Yun, Z., Zhao, L., & Wu, Q. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2225 · Cited by 12 · see citing works
Hartman, M. D., Figueroa, C. M., Arias, D. G., & Iglesias, A. Á. (2016) · Plant and Cell Physiology · doi:10.1093/pcp/pcw180 · Cited by 12 · see citing works
Figueroa, C. M., & Iglesias, A. Á. (2009) · Biochimie · doi:10.1016/j.biochi.2009.09.013 · Cited by 11 · see citing works
Cloning, expression, and characterization of a novel xylose reductase from Rhizopus oryzae
Zhang, M., Jiang, S., Zheng, Z. X., Li, X., Luo, S., & Wu, X. (2015) · Journal of Basic Microbiology · doi:10.1002/jobm.201400786 · Cited by 10 · see citing works
Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase
Lü, M., Huang, Y., White, M. A., Wu, X., Liu, N., Cheng, X., & Chen, Y. (2012) · Chemical Communications · doi:10.1039/c2cc36334h · Cited by 10 · see citing works
Structural and mutational studies on an aldo‐keto reductase AKR5C3 from G luconobacter oxydans
Liu, X., Wang, C., Zhang, L., Yao, Z., Cui, D., Wu, L., Lin, J., Yuan, Y. A., & Wei, D. (2014) · Protein Science · doi:10.1002/pro.2531 · Cited by 8 · see citing works
Zhang, W., Chang, X., Han, Y., Li, T., Dou, J., Du, W., Wu, W., Wang, W., Zhang, Z., & Sun, C. (2024) · Biological Control · doi:10.1016/j.biocontrol.2024.105676 · Cited by 7 · see citing works
Zhang, S., Zhang, Y., Kong, W., Guo, W., Yuan, Q., Jiang, Y., & Liu, Y. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.161964 · Cited by 7 · see citing works
Reductive enzymatic dynamic kinetic resolution affording 115 g/L (S)-2-phenylpropanol
Rapp, C., Pival-Marko, S., Tassano, E., Nidetzky, B., & Kratzer, R. (2021) · BMC Biotechnology · doi:10.1186/s12896-021-00715-5 · Cited by 7 · see citing works
Self-citationExpression of AKRs superfamily and prognostic in human gastric cancer
Yujin, Z., Lin, Y., Li, W., Liu, Q., Gong, H., Li, Y., & Luo, D. (2023) · Medicine · doi:10.1097/md.0000000000033041 · Cited by 7 · see citing works
Zheng, C., Wang, Z., Wang, Q., Shenyong, W., Lao, S., He, J., & Chen, Z. (2021) · Molecular Catalysis · doi:10.1016/j.mcat.2021.111639 · Cited by 7 · see citing works
Reduced genome size ofHelicobacter pylorioriginating from East Asia
Dong, Q. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i19.5666 · Cited by 6 · see citing works
Minen, R. I., Bhayani, J. A., Hartman, M. D., Cereijo, A. E., Zheng, Y., Ballicora, M. A., Iglesias, A. Á., Liu, D., & Figueroa, C. M. (2022) · Plant and Cell Physiology · doi:10.1093/pcp/pcac029 · Cited by 5 · see citing works
Gober, R., Wheeler, R., & Rohr, J. (2019) · MedChemComm · doi:10.1039/c9md00066f · Cited by 5 · see citing works
He, M., Zhou, S., Cui, M., Jin, X., Lai, D.-Y., Zhang, S., Wang, Z., & Chen, Z. (2016) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-016-2285-3 · Cited by 5 · see citing works
Role of Phe-114 in substrate specificity ofCandida tenuisxylose reductase (AKR2B5)
Klimacek, M., Kratzer, R., Szekely, M., & Nidetzky, B. (2007) · Biocatalysis and Biotransformation · doi:10.1080/10242420701379775 · Cited by 2 · see citing works
Self-citationPatulin Detoxification by Evolutionarily Divergent Reductases of Gluconobacter oxydans ATCC 621
Abraham, N., Chan, E. T. S., Li, X., Zhu, H., Mats, L., Zhou, T., & Seah, S. Y. K. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c12572 · Cited by 1 · see citing works
Koubara, K., Kim, M., Takenoya, M., Nakanishi, A., Suzuki, M., Azuma, S., Ito, S., Sasaki, Y., Nakamura, A., & Yajima, S. (2026) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbag041 · Cited by 1 · see citing works
Lamichhane, B., Niraula, A., Mérindol, N., Gélinas, S., Lagüe, P., Ricard, S., Germain, H., & Desgagné‐Penix, I. (2026) · The Plant Journal · doi:10.1111/tpj.70910 · Cited by 1 · see citing works
Protein Structure–Function Paradigm in Plant Stress Tolerance
Bhatt, H., Kumar, A., & Bhavesh, N. S. (2013) · doi:10.1002/9783527675265.ch17
Enzymatic Dynamic Reductive Kinetic Resolution Towards 115 g/L (S)-2-PhenylpropanolPreprint
Rapp, C., Pival-Marko, S., Tassano, E., Nidetzky, B., & Kratzer, R. (2021) · Research Square · doi:10.21203/rs.3.rs-183141/v1
Self-citation(2007) · Yeast · doi:10.1002/yea.1326
Rapp, C., Pival-Marko, S., Tassano, E., Nidetzky, B., & Kratzer, R. (2021) · Figshare · doi:10.6084/m9.figshare.16786792
Self-citationMei, J., Yang, Q., Hu, S., Li, Y., Yu, X., & Wu, Z. (2026) · Aquaculture and Fisheries · doi:10.1016/j.aaf.2026.05.006
- Authors
- Kratzer, R., Wilson, D., & Nidetzky, B.
- Affiliations
- Graz University of Technology (AT)
- University of California, Davis (US)
- Venue
- IUBMB Life (International Union of Biochemistry and Molecular Biology: Life)
- Publisher
- Wiley
- Published
- 2006-09-01
- Volume
- 58
- Issue
- 9
- Pages
- 499-507
- ISSN
- 1521-6543 (ISSN-L)
- 1521-6551
- OpenAlex
- W2085321839
- Cited by
- 56
- References
- 45
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 9 · 2019: 5 · 2018: 4 · 2017: 1 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 4 · 2012: 2
- FWCI
- 0.13
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- IUBMB Life (publishedVersion)
- PubMed (publishedVersion)
- Funders
- W. M. Keck Foundation
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- aldo-keto reductase, xylose reductase, Candida tenuis, catalytic mechanism, substrate specificity, structure-function relationship, electrostatic stabilization, active site residues, substrate binding pocket, biocatalyst design
- MeSH terms
- Aldo-Keto Reductases, Alcohol Oxidoreductases, Aldehyde Reductase, Candida, Catalysis, Fungal Proteins, Models, Chemical, Models, Molecular, Protein Binding, Structure-Activity Relationship, Substrate Specificity, Xylose, Crystallography, X-Ray, Static Electricity
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review