A Tyrosine Aminomutase from Rice (Oryza sativa) lsomerizes (S)-α- to (R)-β-Tyrosine with Unique High Enantioselectivity and Retention of Configuration

被引:15
作者
Walter, Tyler [1 ]
King, Zayna [3 ]
Walker, Kevin D. [1 ,2 ]
机构
[1] Michigan State Univ, Dept Chem, E Lansing, MI 48824 USA
[2] Michigan State Univ, Dept Biochem & Mol Biol, E Lansing, MI 48824 USA
[3] CUNY Medgar Evers Coll, Brooklyn, NY 11225 USA
关键词
PHENYLALANINE AMINOMUTASE; BIOSYNTHESIS; MECHANISM; STEREOCHEMISTRY; PATHWAY;
D O I
10.1021/acs.biochem.5b01331
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A recently discovered 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO)-dependent tyrosine aminomutase (OsTAM) from rice [Yan, J., et al. (2015) Plant Cell 27, 1265] converts (S)-alpha-tyrosine to a mixture of (R)- and (S)-beta-tyrosines, with high (94%) enantiomeric excess, which does not change with pH, like it does for two bacterial TAMs. The K-M of 490 mu M and the k(cat) of 0.005 s(-1) are similar for other TAM enzymes. OsTAM is unique and also catalyzes (R)-beta- from (S)-alpha-phenylalanine. OsTAM principally retains the configuration at the reactive C-alpha and C-beta centers during catalysis much like the phenylalanine aminomutase on the Taxol biosynthetic pathway in Taxus plants.
引用
收藏
页码:1 / 4
页数:4
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