Juvenile hormone diol kinase, a calcium-binding protein with kinase activity, from the silkworm, Bombyx mori
Juvenile hormone (JH) diol kinase (JHDK) is an important enzyme involved in the JH degradation pathway. Bombyx mori ( Bommo)-JHDK cDNA (637 bp) contains an open reading frame encoding a 183-amino acid protein, which reveals a high degree of identity to the two previously reported JHDKs. JHDK is simi...
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Veröffentlicht in: | Insect biochemistry and molecular biology 2005-11, Vol.35 (11), p.1235-1248 |
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Sprache: | eng |
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Zusammenfassung: | Juvenile hormone (JH) diol kinase (JHDK) is an important enzyme involved in the JH degradation pathway.
Bombyx mori (
Bommo)-JHDK cDNA (637
bp) contains an open reading frame encoding a 183-amino acid protein, which reveals a high degree of identity to the two previously reported JHDKs. JHDK is similar to GTP-binding proteins with three conserved sequence elements involved in purine nucleotide binding, contains eight
α-helices and three EF-hand motifs, and resembles the three-dimensional model of 2SCP and some other calcium-binding proteins. The
Bommo-JHDK gene has only a single copy in the silkworm haploid genome, contains only one exon, and its 5′-upstream sequence does not have a JH response element. Although
Bommo-JHDK is highly expressed in the gut of the silkworm, its mRNA expression remains at a constant level during larval development suggesting this enzyme is constitutive and not regulated by JH, at least at the transcriptional level. Recombinant
Bommo-JHDK catalyzed the conversion of 10
S-JH diol into JH diol phosphate, confirming its enzymatic function. Recombinant enzyme formed a dimer and had biochemical characteristics similar to other JHDKs.
Bommo-JHDK, a calcium-binding protein with kinase activity, provides unique insights on how JH levels are regulated in the silkworm. |
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ISSN: | 0965-1748 1879-0240 |
DOI: | 10.1016/j.ibmb.2005.06.005 |