A hydrophobic sequence motif common to N-hydroxylating enzymes
نویسندگان
چکیده
منابع مشابه
A hydrophobic sequence motif common to N-hydroxylating enzymes.
The first committed step in the biosynthesis of various bacterial and fur,gal siderophores (low-molecular-weight iron chelators that are produc~ in response '~o iron deficiency) of the hydroxamate type, such as aerobactin, alcaligin an6, ferrichrome, involves N-hydroxylatie a of a primary amino group. This reaction is catalyzed at the expense of NADPH by a family o[ FAD-dependent enzym ~s. Some...
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DNA polymerases cannot start a chain de novo and must rely on priming devices. In general, DNA primases provide free 3'-hydroxyl termini by the synthesis of short oligonucleotides that are base-paired with the template DNA (1). Bacteria, several bacteriophages and plasmids of certain incompatibility groups encode genes specifying DNA primases (2). Recently, two different sets of amino acid sequ...
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AAM-B is a putative methyltransferase that is a resident protein of lipid droplets. We have identified an N-terminal 28 amino acid hydrophobic sequence that is necessary and sufficient for targeting the protein to droplets. This sequence will also insert AAM-B into the endoplasmic reticulum (ER). A similar hydrophobic sequence (1-23) in the cytochrome p450 2C9 cannot substitute for 1-28 and onl...
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ژورنال
عنوان ژورنال: Trends in Biochemical Sciences
سال: 1998
ISSN: 0968-0004
DOI: 10.1016/s0968-0004(97)01166-3