| Name | trehalases |
|---|---|
| Synonyms | Brush border membrane glycoprotein; TRE; TREA; TREH; Trehalase; Trehalase (Brush border membrane glycoprotein) variant; Trehalase precursor; trehalase (brush border membrane glycoprotein)… |
| Name | validamycin |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 9242988 | Temesvari LA, Cotter DA: Trehalase of Dictyostelium discoideum: inhibition by amino-containing analogs of and affinity purification. Biochimie. 1997 Apr;79(4):229-39. Validamycin A, MDL 25,637 and castanospermine were found to be potent, reversible, competitive inhibitors of D discoideum vegetative trehalase in vitro with IC50 values of 1 x 10 (-9) x 10 (-8) M and 1.25 x 10 (-4) M, respectively. |
389(4,6,6,9) | Details |
| 11161063 | Muller J, Aeschbacher RA, Wingler A, Boller T, Wiemken A: and trehalase in Arabidopsis. Plant Physiol. 2001 Feb;125(2):1086-93. Furthermore, we present results on the distribution and activity of trehalase in Arabidopsis and we describe how inhibition of trehalase by validamycin A affects the plants response to exogenous (alpha-D-glucopyranosyl-[1, 1]-alpha-D-glucopyranoside). |
168(2,2,2,8) | Details |
| 7864639 | Kyosseva SV, Kyossev ZN, Elbein AD: Inhibitors of pig kidney trehalase. . Arch Biochem Biophys. 1995 Feb 1;316(2):821-6. Validoxylamine A and validamycin A, two other trehalase inhibitors, showed potent competitive inhibition against purified pig kidney trehalase, with IC50 values of 2.4 x 10 (-9) and 2.5 x 10 (-4) M, respectively. |
86(1,1,1,6) | Details |
| 15907687 | Garcia NA, Iribarne C, Lopez M, Herrera-Cervera JA, Lluch C: Physiological implications of trehalase from Phaseolus vulgaris root nodules: partial purification and characterization. Plant Physiol Biochem. 2005 Apr;43(4):355-61. Epub 2005 Mar 18. The purification and characterization of trehalase from common bean nodules as well as the role of this enzyme on growth, nodulation fixation by examining the effects of the trehalase inhibitor validamycin A, was studied. |
35(0,1,1,5) | Details |
| 9854811 | Knuesel I, Murao S, Shin T, Amachi T, Kayser H: Comparative studies of suidatrestin, a specific inhibitor of trehalases. . Comp Biochem Physiol B Biochem Mol Biol. 1998 Aug;120(4):639-46. Its inhibitory potential was 7 to 50-fold higher than that of validamycin when tested against insect, fungal and mammalian trehalases. |
35(0,1,1,5) | Details |
| 9008394 | Goddijn OJ, Verwoerd TC, Voogd E, Krutwagen RW, de Graaf PT, van Dun K, Poels J, Ponstein AS, Damm B, Pen J: Inhibition of trehalase activity enhances accumulation in transgenic plants. Plant Physiol. 1997 Jan;113(1):181-90. An increase in accumulation, up to 0.41 and 4.04 mg g-1 fresh weight in tobacco leaves and potato micro-tubers, respectively, was noted when the potent trehalase inhibitor validamycin A was added to in vitro plants and to hydroponically grown greenhouse plants. |
33(0,1,1,3) | Details |
| 16751539 | Streeter JG, Gomez ML: Three enzymes for synthesis in Bradyrhizobium cultured bacteria and in bacteroids from soybean nodules. Appl Environ Microbiol. 2006 Jun;72(6):4250-5. Validamycin A, a commonly used trehalase inhibitor, was found to also inhibit TS and MOTS, and other trehalase inhibitors, such as trehazolin, must be used in studies of these enzymes in nodules. |
32(0,1,1,2) | Details |
| 16377847 | Xue YP, Zheng YG, Shen YC: Preparation of trehalase inhibitor validoxylamine A by biocatalyzed hydrolysis of validamycin A with honeybee (Apis cerana Fabr.) beta-glucosidase. Appl Biochem Biotechnol. 2005 Dec;127(3):157-71. |
32(0,1,1,2) | Details |
| 19232773 | Lopez M, Tejera NA, Lluch C: Validamycin A improves the response of Medicago truncatula plants to salt stress by inducing accumulation in the root nodules. J Plant Physiol. 2009 Jul 15;166(11):1218-22. Epub 2009 Feb 20. For this purpose, we used validamycin A, a potent trehalase inhibitor, in order to induce accumulation. |
31(0,1,1,1) | Details |
| 2335220 | Salleh HM, Honek JF: Time-dependent inhibition of porcine kidney trehalase by aminosugars. FEBS Lett. 1990 Mar 26;262(2):359-62. Validamycin A, validoxylamine A and MDL 25,637 were found to be potent, time-dependent inhibitors of the enzyme in vitro. |
3(0,0,0,3) | Details |
| 17455176 | Gibson RP, Gloster TM, Roberts S, Warren RA, Storch de Gracia I, Garcia A, Chiara JL, Davies GJ: Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors. Angew Chem Int Ed Engl. 2007;46(22):4115-9. |
1(0,0,0,1) | Details |
| 3583921 | Asano N, Yamaguchi T, Kameda Y, Matsui K: Effect of validamycins on glycohydrolases of Rhizoctonia solani. J Antibiot. 1987 Apr;40(4):526-32. In particular, validoxylamine A strongly inhibited trehalase in a competitive manner with a Ki value of 1.9 X 10 (-9) M. It was found that validamycin A is transported into the cell and hydrolyzed therein by a beta-glucosidase yielding validoxylamine A with greater inhibitory activity. |
1(0,0,0,1) | Details |
| 18648803 | Choi WS, Wu X, Choeng YH, Mahmud T, Jeong BC, Lee SH, Chang YK, Kim CJ, Hong SK: Genetic organization of the putative salbostatin biosynthetic gene cluster including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus ATCC 21838. Appl Microbiol Biotechnol. 2008 Sep;80(4):637-45. Epub 2008 Jul 22. The cyclization of to 2-epi-5-epi-valiolone, catalyzed by the 2-epi-5-epi-valiolone synthases, is the first committed step in the biosynthesis of C ( 7 ) N-aminocyclitol-containing natural products, such as validamycin and acarbose. The same core unit is also found in salbostatin, a related pseudodisaccharide that has strong trehalase inhibitory activity. |
1(0,0,0,1) | Details |