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References from Structure and evolutionary trace-assisted screening of a residue swapping the substrate ambiguity and chiral specificity in an esterase. Local targets link to admitted publications; unresolved targets remain external evidence.
Environmental assessment of enzyme use in industrial production – a literature review
10.1016/j.jclepro.2012.11.005 · 2013 · External reference
10.1021/acs.chemrev.7b00203
10.1021/acs.chemrev.7b00203 · External reference
Decoding the ocean's microbiological secrets for marine enzyme biodiscovery
2020 · External reference
10.1111/febs.15199
10.1111/febs.15199 · External reference
Relationships between substrate promiscuity and chiral selectivity of esterases from phylogenetically and environmentally diverse microorganisms
10.3390/catal8010010 · 2018 · External reference
10.1002/anie.201907729
10.1002/anie.201907729 · External reference
Study of functional and allosteric sites in protein superfamilies
10.32607/20758251-2015-7-4-34-45 · 2015 · External reference
Protein function machinery: from basic structural units to modulation of activity
10.1016/j.sbi.2016.10.021 · 2017 · External reference
10.1021/acschembio.7b00996
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10.1042/bj20130552
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10.1038/s41598-018-35033-y
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10.1042/bj20101405
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10.1098/rsta.2016.0150
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10.1074/jbc.m116.747527
10.1074/jbc.m116.747527 · External reference
10.1016/j.sbi.2016.07.007
10.1016/j.sbi.2016.07.007 · External reference
Stereodivergent evolution of artificial enzymes for the michael reaction
10.1002/anie.201712554 · 2018 · External reference
10.1073/pnas.0603236103
10.1073/pnas.0603236103 · External reference
10.1093/molbev/msu281
10.1093/molbev/msu281 · External reference
Engineering the enantio-selectivity and thermostability of a (+)-γ-lactamase from Microbacterium hydrocarbonoxydans for kinetic resolution of vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one)
2017 · External reference
Increasing redox potential, redox mediator activity and stability in a fungal laccase by computer-guided mutagenesis and directed evolution
10.1021/acscatal.9b00531 · 2019 · External reference
10.1073/pnas.1901979116
10.1073/pnas.1901979116 · External reference
10.1038/s41929-019-0394-4
10.1038/s41929-019-0394-4 · External reference
10.1016/j.chembiol.2004.10.012
10.1016/j.chembiol.2004.10.012 · External reference
Control of lipase enantio-selectivity by engineering the substrate binding site and access channel
10.1002/cbic.200900439 · 2009 · External reference
10.1021/ja903482u
10.1021/ja903482u · External reference
10.1039/c2dt31833d
10.1039/c2dt31833d · External reference
10.1073/pnas.1915054117
10.1073/pnas.1915054117 · External reference
Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases
2016 · External reference
10.1021/ja311630a
10.1021/ja311630a · External reference
Simultaneous use of in silico design and a correlated mutation network as a tool to efficiently guide enzyme engineering
10.1002/cbic.201402665 · 2015 · External reference
10.1111/febs.15680
10.1111/febs.15680 · External reference
The modular structure of alpha/beta-hydrolases
10.1111/febs.15071 · 2020 · External reference
10.1042/bj20121221
10.1042/bj20121221 · External reference
10.1371/journal.pbio.1002452
10.1371/journal.pbio.1002452 · External reference
Enzyme promiscuity shapes adaptation to novel growth substrates
10.15252/msb.20188462 · 2019 · External reference
10.1006/jmbi.1996.0167
10.1006/jmbi.1996.0167 · External reference
10.1016/j.jmb.2003.12.078
10.1016/j.jmb.2003.12.078 · External reference
10.1073/pnas.0914877107
10.1073/pnas.0914877107 · External reference
Tuning the properties of natural promiscuous enzymes by engineering their nano-environment
10.1021/acsnano.0c08716 · 2020 · External reference
10.1107/s0907444909047337
10.1107/s0907444909047337 · External reference
10.1107/s0907444913000061
10.1107/s0907444913000061 · External reference
10.1107/s0907444910045749
10.1107/s0907444910045749 · External reference
10.1107/s0907444996012255
10.1107/s0907444996012255 · External reference
10.1107/s0907444910007493
10.1107/s0907444910007493 · External reference
10.1107/s0907444909029436
10.1107/s0907444909029436 · External reference
10.1002/(sici)1096-987x(199802)19:3<319::aid-jcc6>3.0.co;2-w
10.1002/(sici)1096-987x(199802)19:3<319::aid-jcc6>3.0.co;2-w · External reference
Fpocket: An open source platform for ligand pocket detection
10.1186/1471-2105-10-168 · 2009 · External reference
10.1101/gr.176214.114
10.1101/gr.176214.114 · External reference
10.1128/jb.00111-06
10.1128/jb.00111-06 · External reference
Quick E. A fast spectrophotometric method to ensure the enantioselectivity of hydrolases
10.1021/jo9707803 · 1997 · External reference
Structural insights of a hormone sensitive lipase homologue Est22
2016 · External reference
Structural and functional analyses of a bacterial homologue of hormone-sensitive lipase from a metagenomic library
10.1107/s0907444913013425 · 2013 · External reference
Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase
10.1038/7576 · 1999 · External reference
Crystal structures of Pseudomonas putida esterase reveal the functional role of residues 187 and 287 in substrate binding and chiral recognition
10.1016/j.bbrc.2014.03.072 · 2014 · External reference
PyETV: A PyMOL evolutionary trace viewer to analyze functional site predictions in protein complexes
10.1093/bioinformatics/btq566 · 2010 · External reference
10.1016/s0022-2836(05)80360-2
10.1016/s0022-2836(05)80360-2 · External reference
UniProt: a worldwide hub of protein knowledge
10.1093/nar/gky1049 · 2019 · External reference
10.1093/nar/gkx1036
10.1093/nar/gkx1036 · External reference
10.1093/bioinformatics/bty386
10.1093/bioinformatics/bty386 · External reference