Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 12, Issue 33, Pages 6354-6358Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4ob01167h
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Funding
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council
- Cancer Research UK
- European Union
- Dulverton Trust
- Biotechnology and Biological Sciences Research Council [BB/L000121/1] Funding Source: researchfish
- BBSRC [BB/L000121/1] Funding Source: UKRI
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2-Oxoglutarate and iron dependent oxygenases have potential for the stereoselective hydroxylation of amino acids and related compounds. The biochemical and kinetic properties of recombinant gamma-butyrobetaine hydroxylase from human and Pseudomonas sp. AK1 were compared. The results reveal differences between the two BBOXs, including in their stimulation by ascorbate. Despite their closely related sequences, the two enzymes also display different substrate selectivities, including for the production of (di)hydroxylated betaines, implying use of engineered BBOXs for biocatalytic purposes may be productive.
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