Comparative kinetics of fatty acid-amino acid conjugate elicitor biosynthesis by midgut tissue microsomes of Lepidopterous caterpillar larvae

Cameron G. Lait, Melanie J. Lobaido, Amy J. Wiester, Sarah Kossak, James Homer Tumlinson, III

Research output: Contribution to journalArticle

Abstract

N-Linolenoyl-L-glutamine is one of several structurally similar fatty acid-amino acid conjugate (FAC) elicitors found in the oral secretions of Lepidopterous caterpillars and its biosynthesis is catalyzed by membrane-associated alimentary tissue enzyme(s). FAC elicitors comprise 17-hydroxylated or non-hydroxylated linolenic acid coupled with L-glutamine or L-glutamate by an amide bond. We demonstrate in vitro biosynthesis of N-linolenoyl-L-glutamine by Manduca sexta, Heliothis virescens, and Helicoverpa zea tissue microsomes. Comparison of N-linolenoyl-L-glutamine biosynthesis kinetics for these species suggests that concurrent biosynthesis and hydrolysis contribute to proportions of FAC elicitors found in their oral secretions. The apparent Km values for coupling of sodium linolenate were 8.75±0.79, 14.3±3.7 and 20.7±3.4 mM and Vmax values were 2.92±0.14, 6.81±1.2 and 4.95±0.55 nmol/min/mg protein for H. zea, H. virescens and M. sexta, respectively. The Km values for coupling of L-glutamine were 10.5±0.26, 22.3±2.0 and 18.9±2.4 mM and Vmax values were 1.78±0.21, 3.71±0.50 and 2.49±0.41 nmol/min/mg of protein for H. zea, H. virescens and M. sexta, respectively.

Original languageEnglish (US)
Pages (from-to)264-274
Number of pages11
JournalArchives of Insect Biochemistry and Physiology
Volume75
Issue number4
DOIs
StatePublished - Dec 1 2010

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Manduca
Biosynthesis
microsomes
Microsomes
midgut
glutamine
Zea mays
Larva
insect larvae
alpha-Linolenic Acid
Fatty Acids
biosynthesis
Heliothis virescens
Helicoverpa zea
Tissue
fatty acids
Glutamine
Manduca sexta
kinetics
Amino Acids

All Science Journal Classification (ASJC) codes

  • Physiology
  • Biochemistry
  • Insect Science

Cite this

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title = "Comparative kinetics of fatty acid-amino acid conjugate elicitor biosynthesis by midgut tissue microsomes of Lepidopterous caterpillar larvae",
abstract = "N-Linolenoyl-L-glutamine is one of several structurally similar fatty acid-amino acid conjugate (FAC) elicitors found in the oral secretions of Lepidopterous caterpillars and its biosynthesis is catalyzed by membrane-associated alimentary tissue enzyme(s). FAC elicitors comprise 17-hydroxylated or non-hydroxylated linolenic acid coupled with L-glutamine or L-glutamate by an amide bond. We demonstrate in vitro biosynthesis of N-linolenoyl-L-glutamine by Manduca sexta, Heliothis virescens, and Helicoverpa zea tissue microsomes. Comparison of N-linolenoyl-L-glutamine biosynthesis kinetics for these species suggests that concurrent biosynthesis and hydrolysis contribute to proportions of FAC elicitors found in their oral secretions. The apparent Km values for coupling of sodium linolenate were 8.75±0.79, 14.3±3.7 and 20.7±3.4 mM and Vmax values were 2.92±0.14, 6.81±1.2 and 4.95±0.55 nmol/min/mg protein for H. zea, H. virescens and M. sexta, respectively. The Km values for coupling of L-glutamine were 10.5±0.26, 22.3±2.0 and 18.9±2.4 mM and Vmax values were 1.78±0.21, 3.71±0.50 and 2.49±0.41 nmol/min/mg of protein for H. zea, H. virescens and M. sexta, respectively.",
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Comparative kinetics of fatty acid-amino acid conjugate elicitor biosynthesis by midgut tissue microsomes of Lepidopterous caterpillar larvae. / Lait, Cameron G.; Lobaido, Melanie J.; Wiester, Amy J.; Kossak, Sarah; Tumlinson, III, James Homer.

In: Archives of Insect Biochemistry and Physiology, Vol. 75, No. 4, 01.12.2010, p. 264-274.

Research output: Contribution to journalArticle

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T1 - Comparative kinetics of fatty acid-amino acid conjugate elicitor biosynthesis by midgut tissue microsomes of Lepidopterous caterpillar larvae

AU - Lait, Cameron G.

AU - Lobaido, Melanie J.

AU - Wiester, Amy J.

AU - Kossak, Sarah

AU - Tumlinson, III, James Homer

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Y1 - 2010/12/1

N2 - N-Linolenoyl-L-glutamine is one of several structurally similar fatty acid-amino acid conjugate (FAC) elicitors found in the oral secretions of Lepidopterous caterpillars and its biosynthesis is catalyzed by membrane-associated alimentary tissue enzyme(s). FAC elicitors comprise 17-hydroxylated or non-hydroxylated linolenic acid coupled with L-glutamine or L-glutamate by an amide bond. We demonstrate in vitro biosynthesis of N-linolenoyl-L-glutamine by Manduca sexta, Heliothis virescens, and Helicoverpa zea tissue microsomes. Comparison of N-linolenoyl-L-glutamine biosynthesis kinetics for these species suggests that concurrent biosynthesis and hydrolysis contribute to proportions of FAC elicitors found in their oral secretions. The apparent Km values for coupling of sodium linolenate were 8.75±0.79, 14.3±3.7 and 20.7±3.4 mM and Vmax values were 2.92±0.14, 6.81±1.2 and 4.95±0.55 nmol/min/mg protein for H. zea, H. virescens and M. sexta, respectively. The Km values for coupling of L-glutamine were 10.5±0.26, 22.3±2.0 and 18.9±2.4 mM and Vmax values were 1.78±0.21, 3.71±0.50 and 2.49±0.41 nmol/min/mg of protein for H. zea, H. virescens and M. sexta, respectively.

AB - N-Linolenoyl-L-glutamine is one of several structurally similar fatty acid-amino acid conjugate (FAC) elicitors found in the oral secretions of Lepidopterous caterpillars and its biosynthesis is catalyzed by membrane-associated alimentary tissue enzyme(s). FAC elicitors comprise 17-hydroxylated or non-hydroxylated linolenic acid coupled with L-glutamine or L-glutamate by an amide bond. We demonstrate in vitro biosynthesis of N-linolenoyl-L-glutamine by Manduca sexta, Heliothis virescens, and Helicoverpa zea tissue microsomes. Comparison of N-linolenoyl-L-glutamine biosynthesis kinetics for these species suggests that concurrent biosynthesis and hydrolysis contribute to proportions of FAC elicitors found in their oral secretions. The apparent Km values for coupling of sodium linolenate were 8.75±0.79, 14.3±3.7 and 20.7±3.4 mM and Vmax values were 2.92±0.14, 6.81±1.2 and 4.95±0.55 nmol/min/mg protein for H. zea, H. virescens and M. sexta, respectively. The Km values for coupling of L-glutamine were 10.5±0.26, 22.3±2.0 and 18.9±2.4 mM and Vmax values were 1.78±0.21, 3.71±0.50 and 2.49±0.41 nmol/min/mg of protein for H. zea, H. virescens and M. sexta, respectively.

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