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Plastics degradation by hydrolytic enzymes: The plastics‐active enzymes database—PAZy
Open accessAbstract
Petroleum‐based plastics are durable and accumulate in all ecological niches. Knowledge on enzymatic degradation is sparse. Today, less than 50 verified plastics‐active enzymes are known. First examples of enzymes acting on the polymers polyethylene terephthalate (PET) and polyurethane (PUR) have been reported together with a detailed biochemical and structural description. Furthermore, very few polyamide (PA) oligomer active enzymes are known. In this article, the current known enzymes acting on the synthetic polymers PET and PUR are briefly summarized, their published activity data were collected and integrated into a comprehensive open access database. The Plastics‐Active Enzymes Database (PAZy) represents an inventory of known and experimentally verified enzymes that act on synthetic fossil fuel‐based polymers. Almost 3000 homologs of PET‐active enzymes were identified by profile hidden Markov models. Over 2000 homologs of PUR‐active enzymes were identified by BLAST. Based on multiple sequence alignments, conservation analysis identified the most conserved amino acids, and sequence motifs for PET‐ and PUR‐active enzymes were derived.
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Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Cytoscape: A software Environment for integrated models of biomolecular interaction networks
Shannon, P., Markiel, A., Ozier, O., Baliga, N. S., Wang, J. T., Ramage, D., Amin, N., Schwikowski, B., & Ideker, T. (2003) · Genome Research · doi:10.1101/gr.1239303 · Cited by 51,888
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T. J., Karplus, K., Li, W., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,355
Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences
Li, W., & Godzik, A. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl158 · Cited by 11,410
Needleman, S. B., & Wunsch, C. D. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90057-4 · Cited by 11,288
Cd-hit: Accelerated for clustering the next-generation sequencing data
Fu, L., Niu, B., Zhu, Z., Wu, S., & Li, W. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts565 · Cited by 11,175
Exploring Network Structure, Dynamics, and Function Using NetworkX
Hagberg, A. A., Schult, D. A., & Swart, P. J. (2008) · Proceedings of the Python in Science Conference · doi:10.25080/tcwv9851 · Cited by 7,477
T-coffee: a novel method for fast and accurate multiple sequence alignment 1 1Edited by J. Thornton
Notredame, C., Higgins, D. G., & Heringa, J. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4042 · Cited by 6,852
A bacterium that degrades and assimilates poly(ethylene terephthalate)
Yoshida, S., Hiraga, K., Takehana, T., Taniguchi, I., Yamaji, H., Maeda, Y., Toyohara, K., Miyamoto, K., Kimura, Y., & Oda, K. (2016) · Science · doi:10.1126/science.aad6359 · Cited by 3,367
An engineered PET depolymerase to break down and recycle plastic bottles
Tournier, V., Topham, C. M., Gilles, A., David, B., Folgoas, C., Moya-Leclair, E., Kamionka, E., Desrousseaux, M.-L., Texier, H., Gavalda, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2149-4 · Cited by 2,176
Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., et al. (1992) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/5.3.197 · Cited by 2,120
Database resources of the National Center for Biotechnology Information
Coordinators, N. R., Agarwala, R., Barrett, T., Beck, J., Benson, D. A., Bollin, C., Bolton, E., Bourexis, D., Brister, J. R., Bryant, S. H., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gkx1095 · Cited by 1,502
Amaral-Zettler, L. A., Zettler, E. R., & Mincer, T. J. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0308-0 · Cited by 1,407
Characterization and engineering of a plastic-degrading aromatic polyesterase
Austin, H. P., Allen, M. D., Donohoe, B. S., Rorrer, N. A., Kearns, F. L., Silveira, R. L., Pollard, B. C., Dominick, G., Duman, R., El Omari, K., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718804115 · Cited by 1,079
Webb, H., Arnott, J., Crawford, R., & Ivanova, E. (2012) · Polymers · doi:10.3390/polym5010001 · Cited by 958
Plastics: Environmental and Biotechnological Perspectives on Microbial Degradation
Danso, D., Chow, J., & Streit, W. R. (2019) · Applied and Environmental Microbiology · doi:10.1128/aem.01095-19 · Cited by 918
Self-citationMicrobial enzymes for the recycling of recalcitrant petroleum‐based plastics: how far are we?
Wei, R., & Zimmermann, W. (2017) · Microbial Biotechnology · doi:10.1111/1751-7915.12710 · Cited by 865
Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation
Joo, S., Cho, I. J., Seo, H., Son, H. F., Sagong, H.-Y., Shin, T. J., Choi, S. Y., Lee, S. Y., & Kim, K.-J. (2018) · Nature Communications · doi:10.1038/s41467-018-02881-1 · Cited by 802
Sulaiman, S., Yamato, S., Kanaya, E., Kim, J.-J., Koga, Y., Takano, K., & Kanaya, S. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.06725-11 · Cited by 711
Cutinase-Catalyzed Hydrolysis of Poly(ethylene terephthalate)
Ronkvist, Å. M., Xie, W., Lu, W., & Gross, R. A. (2009) · Macromolecules · doi:10.1021/ma9005318 · Cited by 708
Müller, R., Schrader, H., Profe, J., Dresler, K., & Deckwer, W. (2005) · Macromolecular Rapid Communications · doi:10.1002/marc.200500410 · Cited by 670
Son, H. F., Cho, I. J., Joo, S., Seo, H., Sagong, H.-Y., Choi, S. Y., Lee, S. Y., & Kim, K.-J. (2019) · ACS Catalysis · doi:10.1021/acscatal.9b00568 · Cited by 572
Structural insight into catalytic mechanism of PET hydrolase
Han, X., Liu, W., Huang, J.-W., Ma, J., Zheng, Y., Ko, T.-P., Xu, L., Cheng, Y.-S., Chen, C.-C., & Guo, R.-T. (2017) · Nature Communications · doi:10.1038/s41467-017-02255-z · Cited by 544
Biodegradation of polyesters containing aromatic constituents
Müller, R.-J., Kleeberg, I., & Deckwer, W.-D. (2001) · Journal of Biotechnology · doi:10.1016/s0168-1656(00)00407-7 · Cited by 497
Microplastics provide new microbial niches in aquatic environments
Yang, Y., Liu, W., Zhang, Z., Grossart, H.-P., & Gadd, G. M. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10704-x · Cited by 447
Danso, D., Schmeisser, C., Chow, J., Zimmermann, W., Wei, R., Leggewie, C., Li, X., Hazen, T., & Streit, W. R. (2018) · Applied and Environmental Microbiology · doi:10.1128/aem.02773-17 · Cited by 445
Self-citationHerrero Acero, E., Ribitsch, D., Steinkellner, G., Gruber, K., Greimel, K., Eiteljoerg, I., Trotscha, E., Wei, R., Zimmermann, W., Zinn, M., et al. (2011) · Macromolecules · doi:10.1021/ma200949p · Cited by 420
Kawai, F., Oda, M., Tamashiro, T., Waku, T., Tanaka, N., Yamamoto, M., Mizushima, H., Miyakawa, T., & Tanokura, M. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5860-y · Cited by 354
Evaluation of biological degradation of polyurethanes
Magnin, A., Pollet, E., Phalip, V., & Avérous, L. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107457 · Cited by 352
Bollinger, A., Thies, S., Knieps-Grünhagen, E., Gertzen, C., Kobus, S., Höppner, A., Ferrer, M., Gohlke, H., Smits, S. H. J., & Jaeger, K.-E. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00114 · Cited by 320
Carniel, A., Valoni, É., Nicomedes, J., Gomes, A. D. C., & Castro, A. M. D. (2017) · Process Biochemistry · doi:10.1016/j.procbio.2016.07.023 · Cited by 316
The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function
Lasica, A. M., Ksiazek, M., Madej, M., & Potempa, J. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00215 · Cited by 312
Active Site Flexibility as a Hallmark for Efficient PET Degradation by I. sakaiensis PETase
Fecker, T., Galaz-Davison, P., Engelberger, F., Narui, Y., Sotomayor, M., Parra, L. P., & Ramírez-Sarmiento, C. A. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.02.005 · Cited by 290
The Plastisphere – Uncovering tightly attached plastic “specific” microorganisms
Kirstein, I. V., Wichels, A., Gullans, E., Krohne, G., & Gerdts, G. (2019) · PLOS ONE · doi:10.1371/journal.pone.0215859 · Cited by 276
Roth, C., Wei, R., Oeser, T., Then, J., Föllner, C., Zimmermann, W., & Sträter, N. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5672-0 · Cited by 260
Colour- and form-dependent loss of plastic micro-debris from the North Pacific Ocean
Shaw, D. G., & Day, R. H. (1994) · Marine Pollution Bulletin · doi:10.1016/0025-326x(94)90184-8 · Cited by 260
Wei, R., Oeser, T., Schmidt, J., Meier, R., Barth, M., Then, J., & Zimmermann, W. (2016) · Biotechnology and Bioengineering · doi:10.1002/bit.25941 · Cited by 248
Identification and Characterization of Bacterial Cutinase
Chen, S., Tong, X., Woodard, R. W., Du, G., Wu, J., & Chen, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800848200 · Cited by 242
Microbial synthesis of vanillin from waste poly(ethylene terephthalate)
Sadler, J. C., & Wallace, S. (2021) · Green Chemistry · doi:10.1039/d1gc00931a · Cited by 237
Furukawa, M., Kawakami, N., Tomizawa, A., & Miyamoto, K. (2019) · Scientific Reports · doi:10.1038/s41598-019-52379-z · Cited by 234
Shirke, A. N., White, C., Englaender, J. A., Zwarycz, A., Butterfoss, G. L., Linhardt, R. J., & Gross, R. A. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01189 · Cited by 233
Suen, G., Weimer, P. J., Stevenson, D. M., Aylward, F. O., Boyum, J., Deneke, J., Drinkwater, C., Ivanova, N. N., Mikhailova, N., Chertkov, O., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018814 · Cited by 231
Kleeberg, I., Hetz, C., Kroppenstedt, R. M., Müller, R.-J., & Deckwer, W.-D. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.5.1731-1735.1998 · Cited by 213
Phylogenetic Distribution of Plastic-Degrading Microorganisms
Gambarini, V., Pantos, O., Kingsbury, J. M., Weaver, L., Handley, K. M., & Lear, G. (2021) · mSystems · doi:10.1128/msystems.01112-20 · Cited by 210
Genome Sequence and Analysis of the Soil Cellulolytic Actinomycete Thermobifida fusca YX
Lykidis, A., Mavromatis, K., Ivanova, N., Anderson, I., Land, M., DiBartolo, G., Martinez, M., Lapidus, A., Lucas, S., Copeland, A., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.01899-06 · Cited by 209
Hydrolysis of polyethyleneterephthalate by p‐nitrobenzylesterase from Bacillus subtilis
Ribitsch, D., Heumann, S., Trotscha, E., Herrero Acero, E., Greimel, K., Leber, R., Birner‐Gruenberger, R., Deller, S., Eiteljoerg, I., Remler, P., et al. (2011) · Biotechnology Progress · doi:10.1002/btpr.610 · Cited by 204
Degradation of Polyester Polyurethane by Bacterial Polyester Hydrolases
Schmidt, J., Wei, R., Oeser, T., Dedavid e Silva, L., Breite, D., Schulze, A., & Zimmermann, W. (2017) · Polymers · doi:10.3390/polym9020065 · Cited by 203
Pleiss, J., Fischer, M., Peiker, M., Thiele, C., & Schmid, R. D. (2000) · Journal of Molecular Catalysis B: Enzymatic · doi:10.1016/s1381-1177(00)00092-8 · Cited by 195
Self-citationCrystal Structure and Thermodynamic and Kinetic Stability of Metagenome-Derived LC-Cutinase
Sulaiman, S., You, D.-J., Kanaya, E., Koga, Y., & Kanaya, S. (2014) · Biochemistry · doi:10.1021/bi401561p · Cited by 194
Ribitsch, D., Herrero Acero, E., Greimel, K., Dellacher, A., Zitzenbacher, S., Marold, A., Rodriguez, R. D., Steinkellner, G., Gruber, K., Schwab, H., et al. (2012) · Polymers · doi:10.3390/polym4010617 · Cited by 193
Alves, N. M., Mano, J. F., Balaguer, E., Meseguer Dueñas, J. M., & Gómez Ribelles, J. L. (2002) · Polymer · doi:10.1016/s0032-3861(02)00236-7 · Cited by 191
Wei, R., Oeser, T., Then, J., Kühn, N., Barth, M., Schmidt, J., & Zimmermann, W. (2014) · AMB Express · doi:10.1186/s13568-014-0044-9 · Cited by 187
Kleeberg, I., Welzel, K., VandenHeuvel, J., Müller, R.-J., & Deckwer, W.-D. (2005) · Biomacromolecules · doi:10.1021/bm049582t · Cited by 174
Biodegradation of a polyurethane in vitro
Phua, S. K., Castillo, E., Anderson, J. M., & Hiltner, A. (1987) · Journal of Biomedical Materials Research · doi:10.1002/jbm.820210207 · Cited by 172
PMBD: a Comprehensive Plastics Microbial Biodegradation Database
Gan, Z., & Zhang, H. (2019) · Database · doi:10.1093/database/baz119 · Cited by 166
Self-citationHu, X., Thumarat, U., Zhang, X., Tang, M., & Kawai, F. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2555-x · Cited by 164
Bumba, L., Mašín, J., Macek, P., Wald, T., Motlova, L., Bibova, I., Klímová, N., Bednářová, L., Veverka, V., Kachala, M., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.018 · Cited by 163
Xi, X., Ni, K., Hao, H., Shang, Y., Zhao, B. Y., & Qian, Z. (2020) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2020.109715 · Cited by 153
Plastic-Degrading Potential across the Global Microbiome Correlates with Recent Pollution Trends
Zrimec, J., Kokina, M., Jonasson, S., Zorrilla, F., & Zelezniak, A. (2021) · mBio · doi:10.1128/mbio.02155-21 · Cited by 153
The long-term legacy of plastic mass production
Hohn, S., Acevedo‐Trejos, E., Abrams, J. F., de Moura, J. F., Spranz, R., & Merico, A. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.141115 · Cited by 139
The modular structure of α/β‐hydrolases
Bauer, T. L., Buchholz, P. C. F., & Pleiss, J. (2019) · FEBS Journal · doi:10.1111/febs.15071 · Cited by 137
Self-citationOda, M., Yamagami, Y., Inaba, S., Oida, T., Yamamoto, M., Kitajima, S., & Kawai, F. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9374-x · Cited by 132
Day, M., & Wiles, D. M. (1972) · Journal of Applied Polymer Science · doi:10.1002/app.1972.070160117 · Cited by 129
Wei, R., Song, C., Gräsing, D., Schneider, T., Bielytskyi, P., Böttcher, D., Matysik, J., Bornscheuer, U. T., & Zimmermann, W. (2019) · Nature Communications · doi:10.1038/s41467-019-13492-9 · Cited by 127
Liu, C., Shi, C., Zhu, S., Wei, R., & Yin, C. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.11.148 · Cited by 116
Kitadokoro, K., Thumarat, U., Nakamura, R., Nishimura, K., Karatani, H., Suzuki, H., & Kawai, F. (2012) · Polymer Degradation and Stability · doi:10.1016/j.polymdegradstab.2012.02.003 · Cited by 105
Ribitsch, D., Hromić‐Jahjefendić, A., Zitzenbacher, S., Zartl, B., Gamerith, C., Pellis, A., Jungbauer, A., Łyskowski, A., Steinkellner, G., Gruber, K. F., et al. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26372 · Cited by 87
Cloning and sequence analysis of a polyurethane esterase of Comamonas acidovorans TB-35
Nomura, N., Akutsu, Y., Nakajima‐Kambe, T., & Nakahara, T. (1998) · Journal of Fermentation and Bioengineering · doi:10.1016/s0922-338x(99)89001-1 · Cited by 79
Howard, G. T., Crother, B. I., & Vicknair, J. (2001) · International Biodeterioration & Biodegradation · doi:10.1016/s0964-8305(01)00042-7 · Cited by 77
Arntzen, M. Ø., Várnai, A., Mackie, R. I., Eijsink, V. G. H., & Pope, P. B. (2017) · Environmental Microbiology · doi:10.1111/1462-2920.13770 · Cited by 76
Viljakainen, V. R., & Hug, L. A. (2021) · Environmental Microbiology · doi:10.1111/1462-2920.15409 · Cited by 74
Zhang, H., Pérez-García, P., Dierkes, R. F., Applegate, V. M., Schumacher, J., Chibani, C. M., Sternagel, S., Preuss, L., Weigert, S., Schmeisser, C., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.803896 · Cited by 70
Self-citationStructural insights into the unique polylactate‐degrading mechanism of Thermobifida alba cutinase
Kitadokoro, K., Kakara, M., Matsui, S., Osokoshi, R., Thumarat, U., Kawai, F., & Kamitani, S. (2019) · FEBS Journal · doi:10.1111/febs.14781 · Cited by 59
Raut, M. P., Couto, N. A. S., Karunakaran, E., Biggs, C. A., & Wright, P. C. (2019) · Scientific Reports · doi:10.1038/s41598-019-52675-8 · Cited by 54
Production of a recombinant polyester-cleaving hydrolase from Thermobifida fusca in Escherichia coli
Dresler, K., van den Heuvel, J., Müller, R., & Deckwer, W. (2006) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-006-0069-9 · Cited by 53
do Canto, V. P., Thompson, C. E., & Netz, P. A. (2019) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2019.03.001 · Cited by 49
Effects of flax lignin addition on enzymatic oxidation of poly(ethylene adipate) urethanes
Ignat, M.-E., Ignat, M.-E., Ciobanu, C., Doroftei, F., & Popa, V. (2011) · Industrial Crops and Products · doi:10.1016/j.indcrop.2011.03.010 · Cited by 34
Emori, M., Numoto, N., Senga, A., Bekker, G., Kamiya, N., Kobayashi, Y., Ito, N., Kawai, F., & Oda, M. (2020) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26034 · Cited by 28
Functional Annotation of Fibrobacter succinogenes S85 Carbohydrate Active Enzymes
Brumm, P. J., Mead, D. A., Boyum, J., Drinkwater, C., Gowda, K., Stevenson, D., & Weimer, P. J. (2010) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-010-9070-5 · Cited by 27
Environmental Degradation of Poly ( ethylene Terephthalate )
Mohammadian, M., Allen, N. S., Edge, M., & Jones, K. (1991) · Textile Research Journal · doi:10.1177/004051759106101109 · Cited by 26
A new arylesterase from Pseudomonas pseudoalcaligenes can hydrolyze ionic phthalic polyesters
Haernvall, K., Zitzenbacher, S., Yamamoto, M., Schick, M. B., Ribitsch, D., & Guebitz, G. M. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.01.012 · Cited by 21
Computational studies of polyurethanases from Pseudomonas
do Canto, V. P., Thompson, C. E., & Netz, P. A. (2021) · Journal of Molecular Modeling · doi:10.1007/s00894-021-04671-x · Cited by 9
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(2026) · doi:10.1128/aem.01698-25
Metadata
- Authors
- Buchholz, P. C. F., Feuerriegel, G., Zhang, H., Perez‐Garcia, P., Nover, L., Chow, J., Streit, W. R., & Pleiss, J.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 2022-02-25
- Volume
- 90
- Issue
- 7
- Pages
- 1443-1456
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W4213330195
- Cited by
- 259
- References
- 83
- FWCI
- 19.05
- Type
- journal article
- Language
- en
- Open access
- hybrid
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