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Virginia Tech

Maize β-glucosidase substrate specificity and natural substrates

Abstract

dc:description.abstract

Plant β-glucosidases (β-D-glucoside glucohydrolases, E.C. 3.2.1.21) are known to function in defense in cyanogenic systems, and may also function in the metabolism of phytohormone glucosides and glucosides of other secondary plant products. Maize (Zea mays L.) β-glucosidase is a homodimer of 60 KD monomers and occurs in the plastid. Numerous glycosides were tested as substrates and K<sub>m</sub>'s and V<sub>m</sub>'s were determined. Various compounds were also tested as inhibitors and K<sub>i</sub>'s and/or K<sub>i</sub>’ 's were estimated. 4- methylumbelliferyl-β-D-glucoside was the best substrate (K<sub>m</sub>=0.14 mM) for which kinetic data were obtained. Monosaccharides were poor inhibitors. The best competitive inhibitors were D-gluconic acid lactone, dhurrin, and 2,4- dihydroxy-7-methoxy-2H-1, 4-benzoxazin-3(4H)-one (DIMBOA) (K<sub>i</sub>'s< 1 mM). The enzyme had broad substrate specificity and could cleave many glycosides with hydrophobic aglycones. One major substrate, the hydroxamic acid 2,4-dihydroxy-7- methoxy-1, 4-benzoxazin-3-one-8-D-glucopyranoside (DIMBOA-glc), was found in methanolic maize extracts. Increasing DIMBOA levels are associated with increasing resistance to several pests. The highest levels of enzyme activity and hydroxamic acids along K55 and H95 shoot length were found near the node. Tissue distribution of hydroxamic acids and β-glucosidase activity was also determined. In K55, both were found in the stele of the mesocotyl, the young leaves, and associated with the vascular bundles of the coleoptile. A major function of the enzyme is to mediate insect and pathogen resistance via the release of the toxic aglycone DIMBOA.

Degree

thesis:*
Name thesis:degree_name
Master of Science
Level thesis:degree_level
masters
Discipline thesis:degree_discipline
Biology
Department dc:contributor.department
Biology
Grantor dc:publisher
Virginia Tech
Year dc:date.issued
1993

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Babcock, Gwen
Chair dc:contributor.committeechair
  • Esen, Asim
Committee members dc:contributor.committeemember
  • Cramer, Carole L.
  • Johnson, John L.
  • Rutherford, Charles L.
  • Saghai-Maroof, Mohammad A.

Rights

dc:rights
Statement dc:rights
  • In Copyright
Language dc:language.iso
en

Identifiers

dc:identifier.*
Dc Identifier Other
etd-10312009-020235
OAI identifier oai:identifier
oai:vtechworks.lib.vt.edu:10919/45360

Chain of custody

source
Harvested from
Virginia Tech
Base URL
vtechworks.lib.vt.edu/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
related terms
citation

Babcock, Gwen. Maize β-glucosidase substrate specificity and natural substrates. masters thesis, Virginia Tech, 1993. http://hdl.handle.net/10919/45360