Biochemistry of proteins that bind and metabolize juvenile hormones.
A diverse group of proteins has evolved to bind and metabolize insect juvenile hormones (JHs). Synthetic radiolabeled JHs and their photoaffinity analogs have enabled us to isolate and characterize JH binding proteins (JHBPs), a putative nuclear JH receptor, JH esterases (JHEs), JH epoxide hydrolases (JHEHs), and methyl farnesoate binding proteins (MFBPs). Highlights of recent progress on structural characterization of JHBPs and JHEHs of two lepidopterans will be described. Efforts to identify MFBPs of penaeid shrimp will be discussed, and the discovery of a possible vertebrate JHBP will be presented.
Prestwich
G D
GD
Department of Chemistry, University at Stony Brook, NY 11794-3400, USA.
Wojtasek
H
H
Lentz
A J
AJ
Rabinovich
J M
JM
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D004851:Epoxide Hydrolases / Q000378:metabolism; D005231:Fatty Acids, Unsaturated / Q000378:metabolism; D006801:Humans; D019476:Insect Proteins; D007605:Juvenile Hormones / Q000378:metabolism*; D008969:Molecular Sequence Data; D011956:Receptors, Cell Surface / Q000378:metabolism
D002352:Carrier Proteins; D005231:Fatty Acids, Unsaturated; D019476:Insect Proteins; D007605:Juvenile Hormones; D011956:Receptors, Cell Surface; C035606:juvenile hormone-binding protein, insect; C032429:methyl farnesoate; D004851:Epoxide Hydrolases; C055698:juvenile hormone epoxide hydrolase