Comparison of the substrate selectivity and biochemical properties of human and bacterial γ-butyrobetaine hydroxylase

被引:19
作者
Rydzik, Anna M. [1 ]
Leung, Ivanhoe K. H. [1 ]
Kochan, Grazyna T. [2 ]
Loik, Nikita D. [1 ]
Henry, Luc [1 ]
McDonough, Michael A. [1 ]
Claridge, Timothy D. W. [1 ]
Schofield, Christopher J. [1 ]
机构
[1] Univ Oxford, Dept Chem, Chem Res Lab, Oxford OX1 3TA, England
[2] Univ Oxford, Struct Genom Consortium, Headington OX3 7DQ, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
CARNITINE BIOSYNTHESIS; PROLINE HYDROXYLASES; ALARM PHEROMONE; METABOLISM; ANTHOPLEURINE; MILDRONATE; MAMMALS; ACID;
D O I
10.1039/c4ob01167h
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
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.
引用
收藏
页码:6354 / 6358
页数:5
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