Membrane-bound trehalase from cecropia silkmoth muscle

Gussin, Arnold E.S.; Wyatt, G.R.

doi:10.1016/0003-9861(65)90106-2

Cited by 79 publications

(11 citation statements)

References 18 publications

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“…Two types of trehalases, soluble and bound ones, have been found in the European honeybee, 18) Apis mellifera, and silkworm, 19) Bombix mori. In our previous studies, 4,20) the bound-type trehalase was purified from European honeybees, and the kinetic properties of the hydrolytic reaction, molecular cloning of the cDNA, and the gene structure in chromosome were examined.…”

Section: )mentioning

confidence: 99%

Catalytic Reaction Mechanism Based on α-Secondary Deuterium Isotope Effects in Hydrolysis of Trehalose by European Honeybee Trehalase

Mori

Lee

Okuyama

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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Section: )mentioning

confidence: 99%

Catalytic Reaction Mechanism Based on α-Secondary Deuterium Isotope Effects in Hydrolysis of Trehalose by European Honeybee Trehalase

Mori

Lee

Okuyama

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…Trehalase in the flight muscle of locusts and other insects with synchronous flight muscles is bound to membranes that appear in the microsomal fraction upon tissue fractionation (Gussin and Wyatt, 1965;Worm, 1981;Vaandrager, 1989), but the exact cellular localization has not yet been established. However, it has been observed that trehalase activity in homogenates of flight muscles from cockroaches, moths and locusts (Zebe and McShan, 1959;Gussin and Wyatt, 1965;Gilby et al, 1967;Candy, 1974) is increased after the disruption of membrane integrity, e.g.…”

Section: Introductionmentioning

confidence: 99%

Long-term effects of the trehalase inhibitor trehazolin on trehalase activity in locust flight muscle

Wegener

Macho

Schlöder

et al. 2010

Journal of Experimental Biology

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SUMMARY Trehalase (EC 3.2.1.28) hydrolyzes the main haemolymph sugar of insects, trehalose, into the essential cellular substrate glucose. Trehalase in locust flight muscle is bound to membranes that appear in the microsomal fraction upon tissue fractionation, but the exact location in vivo has remained elusive. Trehalase has been proposed to be regulated by a novel type of activity control that is based on the reversible transformation of a latent (inactive) form into an overt (active) form. Most trehalase activity from saline-injected controls was membrane-bound (95%) and comprised an overt form (∼25%) and a latent form (75%). Latent trehalase could be assayed only after the integrity of membranes had been destroyed. Trehazolin, a potent tight-binding inhibitor of trehalase, is confined to the extracellular space and has been used as a tool to gather information on the relationship between latent and overt trehalase. Trehazolin was injected into the haemolymph of locusts, and the trehalase activity of the flight muscle was determined at different times over a 30-day period. Total trehalase activity in locust flight muscle was markedly inhibited during the first half of the interval, but reappeared during the second half. Inhibition of the overt form preceded inhibition of the latent form, and the time course suggested a reversible precursor–product relation (cycling) between the two forms. The results support the working hypothesis that trehalase functions as an ectoenzyme, the activity of which is regulated by reversible transformation of latent into overt trehalase.

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“…Sactor (24) showed that phloridzin also inhibits UDPG pyrophosplhorylase, a vital enzynme in trehalose biosvnthesis. An inhibitor of trehalase activity in insects, a-methVl-D-mannoside (14), decreased germination and pollen-tube lengths wlhere trehalose was the carbon source, but Inot where sucrose was the source ( Hemerocallis minor and Galtonia candicans T'rehalase was allowed to diffuse from 10 mg of pollen in 1 ml of 1 % NaCl (w/v), pH 6.4, for 24 hr at 40. The preparation was dialyzed against 0.33 % NaCl (w/v) for 5 hr and assayed as in Materials and Methods.…”

Section: Methodsmentioning

confidence: 99%