Table 1.
Experimental dataset description
| Protein name | Length | Temp. (○C) | Mutant name | Temp. (○C) | Mutated residues |
|---|---|---|---|---|---|
| Shble | 124 | Tm: 67.4 | HTS | Tm: 85.1 | G18E,D32V,L63Q,G98V |
| UVF | Tm: 99 | 39 mutations | |||
| Dmeh | 54 | Tm: 49 | |||
| UMC | Tm: 99 | 40 mutations | |||
| β-GUS | 603 | 45 | TR3337 | 65 | Q493R,T509A,M532T,N550S,G559S,N566S |
| mt1 | Tm: 69.7 | A46K,S48R | |||
| BsCSP | 67 | Tm: 53.8 | |||
| mt2 | Tm: 83.7 | M1R,E3K,K65I | |||
| EcHPH | 341 | 51 | hph5 | 67 | D20G,A118V,S225P,Q226L,T246A |
| 12x | 59.7 | V71I,E130K,Q132R,Q137R,I150F,Q215L,R275Q,L276Q,I313L,V315A,A319E,A325V | |||
| PTDH | 355 | 39 | |||
| opt14 | 64.4 | V71I,E130K,Q132K,Q137H,I150F,Q215L,R275L,L276C,I313L,V315A,A319E,A325V,A146S,F198M | |||
| CbADH | 452 | Tm: 65.5 | Q100P | ΔTm: +11.5 | Q100P |
| FAOX | 372 | 37 | FAOX_TE | 45 | T60A,A188G,M244L,N257S,L261M |
| PDAO | 347 | 45 | F42C | 55 | F42C |
| mt18 | ΔTm: +7, | A58E,P65S,Q191R,T271R | |||
| PhyA | 467 | 55 | |||
| mt24 | ΔTm: >+7 | A58E,P65S,Q191R,T271R,E228K,S149P,F131L |
In the first two columns the wild-type protein name and the protein length are reported. In the fourth column, the name of the mutant is reported. Columns 3 and 5 report optimal functional temperatures of the wild-type and the mutated sequence, respectively; Tm when present refers to the melting temperature; column 6 reports the mutated residues. In the case of Dmeh, the two mutants have 39 and 40 mutated residues, respectively (Shah et al., 2007). The considered proteins are: Shble: bleomycin-binding protein from the mesophilic bacterium Streptoalloteichus hindustanus (Brouns et al., 2005); Dmeh: Drosophila melanogaster engrailed homeodomain (Shah et al., 2007); β-GUS: β-glucuronidase (Xiong et al., 2007); BsCSP: cold shock proteins from Bacillus subtilis (Max et al., 2007); EcHPH: Escherichia coli hygromycin B phosphotransferase (Nakamura et al., 2005); PTDH: phosphite dehydrogenase from Pseudomonas stutzeri (Johannes et al., 2005; McLachlan et al., 2007) CbADH: Clostridium beijerinckii alcohol dehydrogenase (Goihberg et al., 2007); FAOX: fructosyl-amino acid oxidase from Corynebacterium sp. (Sakaue and Kajiyama, 2003); pDAO: porcine kidney D-amino acid oxidase (Bakke et al., 2006); PhyA: 3-phytase A from Aspergillus niger (Zhang and Lei, 2007).