Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications
Abstract
:1. Introduction
2. Recent Progress on the Various Reactions Catalyzed by ArMs
2.1. Reduction
2.1.1. Transfer Hydrogenation
2.1.2. Hydrogenation
2.2. Oxidation
2.3. C–C Bond Formation
2.3.1. Cyclopropanation
2.3.2. Friedel–Crafts Reaction
2.3.3. Michael Addition Reaction
2.3.4. Diels–Alder Reaction
2.3.5. Aldol Condensation
2.4. Unnatural Amino Acids
3. Cascade, Sequential, and Synergetic Reactions
4. Rapid Genetic Optimization and Directed Evolution of ArMs
5. Drug Applications
6. Conclusions and Perspectives
Author Contributions
Funding
Conflicts of Interest
References
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Entry | Cofactor (cof) | µM | Protein | Substrate | pH | T (°C) | Time (h) | ee % | TON | Ref |
---|---|---|---|---|---|---|---|---|---|---|
1 | (S)-12 | 190 | No protein | 8 | 7.8 | 30 | 18 | 3R | 101 | [35] |
2 | (S)-12 | 190 | Sav (WT) | 8 | 7.8 | 30 | 18 | 7R | 43 | [35] |
3 | (S)-12 | 190 | Sav(K121A) | 8 | 7.8 | 30 | 18 | 13R | 43 | [35] |
4 | (R)-13 | 190 | No protein | 8 | 7.8 | 30 | 18 | 65R | 110 | [35] |
5 | (R)-13 | 190 | Sav (WT) | 8 | 7.8 | 30 | 18 | 43R | 13 | [35] |
6 | (R)-13 | 190 | Sav (S112M) (cof:Sav = 1.5:4.0) | 8 | 7.8 | 30 | 18 | 68R | 30 | [35] |
7 | (R)-13 | 190 | Sav (S112M) (cof:Sav = 2.5:4.0) | 8 | 7.8 | 30 | 18 | 83R | 33 | [35] |
8 | 14 | 50 | No protein | 8 | 7.0 | 37 | 48 | rac | 65 | [36] |
9 | 14 | 50 | Sav (S112A) | 8 | 7.0 | 37 | 48 | 75R | 142 | [36] |
10 | 14 | 50 | Sav (S112K) | 8 | 7.0 | 37 | 48 | 41S | 100 | [36] |
11 | 14 | 50 | Sav (S112A/K121A) | 8 | 7.0 | 37 | 48 | 59R | 358 | [36] |
12 | 14 | 0.42 | Sav (S112A) @ Ferritin | 8 | 7.0 | 37 | 48 | 46S | 74 | [36] |
13 | 14 | 0.40 | Sav (S112K) @ Ferritin | 8 | 7.0 | 37 | 48 | 47S | 46 | [36] |
14 | 14 | 0.28 | Sav (S112A/K121A) @ Ferritin | 8 | 7.0 | 37 | 48 | 44S | 117 | [36] |
15 | 14 | 10 | No protein | 15 | 7.5 | 37 | 16 | n.d. | 0 | [37] |
16 | 14 | 10 | Sav | 15 | 7.5 | 37 | 16 | 76R | 22 | [37] |
17 | 14 | 10 | Sav_HP46-52 Inserted seq: LSDEDFKAVFGMTRSAFANLPLWKQQHLKKEKGLF | 15 | 7.5 | 37 | 16 | 80R | 162 | [37] |
18 | 14 | 10 | Sav_FPD46-52 Inserted seq: SPLSEALTKANSPAEAYKASRGAG | 15 | 7.5 | 37 | 16 | 82R | 158 | [37] |
19 | 14 | 25 | No protein | 8 | 7.0 | 25 | 24 | rac | 72 | [38] |
20 | 14 | 25 | Sav | 8 | 7.0 | 25 | 24 | 30R | 88 | [38] |
21 | 14 | 25 | scdSav (112SA/121KA/112SB/121KB) | 8 | 7.0 | 25 | 24 | 73R | 176 | [38] |
22 | 14 | 25 | scdSav (112SA/121AA/112RB/121KB) | 8 | 7.0 | 25 | 24 | 96R | 400 | [38] |
23 | 14 | 5 | monovalent scdSav (112SA/121AA/112RB/121KB) | 8 | 7.0 | 50 | 48 | 90R | 17700 | [38] |
24 | 14 | 50 | scdSav (112SA/121KA/112AB/121AB) | 15 | 7.0 | 37 | 48 | 96R | 1976 | [38] |
25 | 14 | 50 | monovalent scdSav (112SA/121AA/112RB/121KB) | 17 | 7.0 | 50 | 48 | 91R | 195 | [38] |
Entry | Metal Source | Host Protein | Modification | [Metal] (µM) | Substrate | Product | tBuOOH (mM) | T (°C) | Time (h) | TON | ee% |
---|---|---|---|---|---|---|---|---|---|---|---|
1 | K2OsO2 | Lysozyme | HA | 30 | 23 | 24 | 110 | 0 | 168 | 289 | 98S |
2 | K2OsO2 | Lysozyme | PA | 30 | 23 | 24 | 110 | 0 | 168 | 85 | 94S |
3 | K2OsO2 | Lysozyme | AA | 30 | 23 | 24 | 110 | 0 | 168 | 103 | 55S |
4 | K2OsO2 | BSA | AA | 30 | 23 | 24 | 110 | 0 | 168 | 275 | 73S |
5 | RuCl3 | Lysozyme | No modification | 60 | 23 | 25 | 220 | 20 | 72 | 361 | 10R |
6 | RuCl3 | Lysozyme | HA | 60 | 23 | 25 | 220 | 20 | 72 | 449 | 56R |
7 | RuCl3 | Lysozyme | PA | 60 | 23 | 25 | 220 | 20 | 72 | 561 | 74R |
8 | RuCl3 | Lysozyme | AA | 60 | 23 | 25 | 220 | 20 | 72 | 749 | 63R |
9 | RuCl3 | BSA | HA | 60 | 23 | 25 | 220 | 20 | 72 | 452 | 88R |
10 | RuCl3 | BSA | HA | 180 | 23 | 25 | 220 | 40 | 72 | 2613 | 82R |
Entry | Cof | Host Protein | [Cof] (µM) | Substrate | pH | T (°C) | Time (h) | TON | de for (E) | ee% (1R,2R) | Ref |
---|---|---|---|---|---|---|---|---|---|---|---|
1 | 31 | No protein | 4.3 | 23, 33 | 8.0 | 25 | 60 | 23 | 62 | n.d. | [55] |
2 | 31 | Mb | 4.3 | 23, 33 | 8.0 | 25 | 60 | 49 | 85 | n.d. | [55] |
3 | 32 | No protein | 4.3 | 23, 33 | 8.0 | 25 | 6 | 9 | 53 | n.d. | [55] |
4 | 32 | Mb | 4.3 | 23, 33 | 8.0 | 25 | 6 | 133 | > 99 | n.d. | [55] |
5 | 31 | No protein | 10 | 33, 35 | 8.0 | 4 | 18 | 51 | >70 | – | [59] |
6 | 31 | LmrR | 10 | 33, 35 | 8.0 | 4 | 18 | 247 | >70 | 17 | [59] |
7 | 31 | LmrR (F93A) | 10 | 33, 35 | 8.0 | 4 | 18 | 232 | >70 | 11 | [59] |
8 | 31 | LmrR (D110A) | 10 | 33, 35 | 8.0 | 4 | 18 | 375 | >70 | 24 | [59] |
9 | 31 | LmrR (W96A) | 10 | 33, 35 | 8.0 | 4 | 18 | 276 | >70 | <5 | [59] |
10 | 31 | LmrR (V15A) | 10 | 33, 35 | 8.0 | 4 | 18 | 15 | >70 | 17 | [59] |
11 | 31 | LmrR (M8A) | 10 | 33, 35 | 8.0 | 4 | 18 | 359 | >70 | 44 | [59] |
12 | 31 | LmrR (M8A) | 10 | 33, 35 | 7.0 | 4 | 18 | 449 | >70 | 51 | [59] |
13 | 31 | No peptide | 20 | 33, 37 | 7.0 | – | 1 | 60 | 70 | 0 | [62] |
14 | 31 | LILHLFL | 20 | 33, 37 | 7.0 | – | 1 | 208 | 68 | –40 | [62] |
15 | 31 | LHLH (l-NMe) FL | 20 | 33, 37 | 7.0 | – | 1 | 64 | 80 | 0 | [62] |
16 | 31 | (d)-LILHLFL | 20 | 33, 37 | 7.0 | – | 1 | 200 | – | 40 | [62] |
Entry | Cof | Protein | [Cof] (µM) | [53] (mM) | [54a] (mM) | Yield (%) | Time (h) | TON | endo/exo | ee (%) for 1S,2R,3R,4R | Ref |
---|---|---|---|---|---|---|---|---|---|---|---|
1 | Cu-Phen 51 | A3-A3′(Y26C) | 30 | 34 | 1 | 21 | 48 | 7.0 | n.d. | 22 | [79] |
2 | Cu-Terpy 52 | A3-A3′(Y26C) | 30 | 34 | 1 | 16 | 48 | 5.3 | n.d. | 14 | [79] |
3 | Cu-Phen 51 | A3-A3′(F119C) | 30 | 34 | 1 | 38 | 48 | 12.7 | 92/8 | 5 | [79] |
4 | Cu-Terpy 52 | A3-A3′(F119C) | 30 | 34 | 1 | 15 | 48 | 5.0 | 93/7 | 52 | [79] |
5 | Cu2+ ion | No protein | 100 | 33 | 1 | 82 | 72 | 8.2 | 92:8 | < 5 | [83] |
6 | Cu2+ ion | NB4 | 100 | 33 | 1 | 16 | 72 | 1.6 | 89:11 | –6 | [83] |
7 | Cu2+ ion | NB4-Pyr 56 | 100 | 33 | 1 | 56 | 72 | 5.6 | 95:5 | 69 | [83] |
8 | Cu2+ ion | NB4-Pyr 56 | 100 | 33 | 0.25 | 94 | 72 | 2.4 | 96:4 | 78 | [83] |
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Himiyama, T.; Okamoto, Y. Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications. Molecules 2020, 25, 2989. https://doi.org/10.3390/molecules25132989
Himiyama T, Okamoto Y. Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications. Molecules. 2020; 25(13):2989. https://doi.org/10.3390/molecules25132989
Chicago/Turabian StyleHimiyama, Tomoki, and Yasunori Okamoto. 2020. "Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications" Molecules 25, no. 13: 2989. https://doi.org/10.3390/molecules25132989