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Substrate Specificity in Thiol Dioxygenases.

Sekotilani Aloi¹, Casey G Davies¹, P Andrew Karplus²

¹Department of Chemistry , University of Otago , P.O. Box 56, Dunedin 9054 , New Zealand.

|May 3, 2019

Summary

This summary is machine-generated.

Thiol dioxygenases catalyze thiol oxidation. Key structural features in cysteine dioxygenase variants dictate substrate specificity for cysteine, 3-mercaptopropionic acid, and mercaptosuccinic acid.

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Area of Science:

Biochemistry
Enzymology
Structural Biology

Background:

Thiol dioxygenases are ferrous iron-dependent enzymes oxidizing thiols to sulfinates.
Existing X-ray structures of cysteine dioxygenase reveal substrate coordination.
Structural data for 3-mercaptopropionate and mercaptosuccinate dioxygenases are lacking.

Purpose of the Study:

To investigate structural determinants of substrate specificity in thiol dioxygenases.
To compare reactivity of enzyme variants with different substrates.
To correlate structural features with enzyme activity.

Main Methods:

Comparative analysis of Rattus norvegicus cysteine dioxygenase variants.
Enzyme activity assays for Pseudomonas aureginosa and Ralstonia eutropha 3-mercaptopropionate dioxygenases.
Correlation of structural variations with substrate specificity.

Main Results:

Three key structural features (cis-peptide bond, residue at position 60, residue at position 164) were identified.
Specific permutations of these features influence substrate binding and reactivity.
Enzyme variants showed altered rates for sulfination of l-cysteine, 3-mercaptopropionic acid, and (R)-mercaptosuccinic acid.

Conclusions:

Structural features significantly impact thiol dioxygenase substrate specificity.
Understanding these features can guide enzyme engineering for specific substrates.
This work provides insights into the catalytic mechanisms and substrate recognition of thiol dioxygenases.