Difficult eval for AI models that predict designed enzyme function
The primary data file is dataset.csv
, which contains the following columns:
kcat
. The experimentally measured turnover number. This has been compared to the baseline of 880 per minute for native BglB and log-transformed.log(mutant/wt)
km
. Experimentally measured Michaelis constant, compared to baseline and transformed by taking the log, so that higher numbers representlog(mutant/wt)
mutant
. The standard biochemical name for the mutant, such as "C167A" to indicate that the cysteine residue at position 167 is replaced with alanine.sequence
the full-length sequence of the mutant. The native sequence is UniProt entry P22505
Predict the scalar value catalytic rate kcat
for designed sequences. Evaluate by Spearman rank correlation.
- In our paper, we achieve 0.57 using an elastic net model on features derived from molecular mechanical simulation of the enzyme–transition state complex.
Predict the scalar value representing substrate binding affinity km
for designed sequences. Evaluate by Spearman rank correlation.
- In our paper, we achieve 0.68 using the same regularized linear model with features from molecular mechanics described above.