KMID : 0545120060160091468
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Journal of Microbiology and Biotechnology 2006 Volume.16 No. 9 p.1468 ~ p.1471
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Sequence-Based Screening for a Putative ¥ã-Butyrobetaine Hydroxylase Gene from Neurospora crassa
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Hur Min-Sang
Cho Jae-Yong
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Abstract
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The last step in L-carnitine biosynthesis in eukaryotic organisms is mediated by -butyrobetaine hydroxylase (EC1.14.11.1), a dioxygenase that converts -butyrobetaine to L-carnitine. This enzyme was previously identified from rat liver and humans, and the peptide sequence of human -butyrobetaine hydroxylase was used to search the Neurospora crassa genome database, which led to an identification of an open reading frame (ORF) consisting of 1,407 bp encoding a polypeptide of 468 amino acids. When this protein was expressed in Saccharomyces cerevisiae, the crude cell-free extract exhibited -butyrobetaine hydroxylase activity.
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KEYWORD
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¥ã-butyrobetaine hydroxylase, Saccharomyces cerevisiae, L-Carnitine, cDNA library, Neurospora crassa
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