Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis
The kinetic properties of L-glutamate:glyoxylate transminase have been investigated. Glycine formation was linear with both protein concentration and incubation time. L-glutamate was the most effective amino donor. Optimal concentrations for L-glutamate and glyoxylate were 150-200 mM and 10-20 mM, r...
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| Otros Autores: | , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
1996
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
| Aporte de: | Registro referencial: Solicitar el recurso aquí |
| LEADER | 05861caa a22007217a 4500 | ||
|---|---|---|---|
| 001 | PAPER-3413 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203252.0 | ||
| 008 | 190411s1996 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0030484653 | |
| 024 | 7 | |2 cas |a aminotransferase, 9031-66-7; glutamic acid, 11070-68-1, 138-15-8, 56-86-0, 6899-05-4; glycine, 56-40-6, 6000-43-7, 6000-44-8; glyoxylic acid, 298-12-4 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a JPPBE | ||
| 100 | 1 | |a Lombardo, M.E. | |
| 245 | 1 | 0 | |a Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis |
| 260 | |c 1996 | ||
| 270 | 1 | 0 | |m Del C Batlle, A.M.Viamonte 1881, 10 A, CP-1056 Buenos Aires, Argentina |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Collins, N., Merrett, M.J., The localization of glycollate-pathway enzymes, Euglena (1975) Biochem. J., 148, pp. 321-328 | ||
| 504 | |a Noguchi, T., Mori, R., Biosynthesis of porphyrin precursors in mammals. Identity of alanine: ,δ-dioxovalerate aminotransferase with alanine: Glyoxylate aminotransferase (1981) J. Biol. Chem., 256, pp. 10335-10339 | ||
| 504 | |a Foley, T., Beale, S.I., δ-Aminolevulinic acid formation from ,δ-dioxovaleric acid in extracts of Euglena gracilis (1982) Plant Physiol., 70, pp. 1495-1502 | ||
| 504 | |a Shioi, Y., Nagamine, M., Sasa, T., Purification and properties of L-alanine:4,5-dioxovalerate aminotransferase from Chlorella regularis (1984) Arch. Biochem. Biophys., 234, pp. 117-124 | ||
| 504 | |a Lombardo, M.E., Araujo, L.S., Juknat, A.A., Del C. Batlle, A.M., Glutmate:4,5-dioxovaleric acid transaminase from Euglena gracilis. Kinetic studies (1989) Eur. J. Biochem., 182, pp. 657-660 | ||
| 504 | |a Varticovski, L., Kushner, J.P., Burnham, B.F., Biosynthesis of porphyrin precursors. Purification and characterization of mammaliam L-alanine: ,δ-dioxovaleric acid aminotransferase (1980) J. Biol. Chem., 255, pp. 3742-3747 | ||
| 504 | |a Lombardo, M.E., Araujo, L.S., Juknat, A.A., Del C. Batlle, A.M., Effect of illumination on growth, chlorophyll content and δ-aminolevulinic acid synthesis in Euglena gracilis (1988) Comp. Biochem. Physiol., 91 B, pp. 279-284 | ||
| 504 | |a Lombardo, M.E., Araujo, L.S., Branca, A., Del C. Batlle, A.M., A method for estimating glycine in the presence of excess glutamate with o-phthaldialdehyde (1990) Z. Naturforsch., 45 C, pp. 911-914 | ||
| 504 | |a Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., Protein measurement with the Polin phenol reagent (1951) J. Biol. Chem., 193, pp. 265-275 | ||
| 504 | |a Kah, A., Dörnemamm, D., Senger, H., Isolation and purification to apparent homogeneity of 4,5-dioxovalerate aminotransferase from Scenedesmus obliquus mutant C-2A′ (1988) Z. Naturforsch., 43 C, pp. 563-571 | ||
| 520 | 3 | |a The kinetic properties of L-glutamate:glyoxylate transminase have been investigated. Glycine formation was linear with both protein concentration and incubation time. L-glutamate was the most effective amino donor. Optimal concentrations for L-glutamate and glyoxylate were 150-200 mM and 10-20 mM, respectively. Initial velocity studies suggested a ping-pong reaction mechanism with a K(m) value of 89.90-66.50 mM for L-glutamate and of 12.50-10.75 mM for glyoxylate. A competitive parabolic substrate inhibition by glyoxylate at concentrations greater than 20 mM was observed. A pure linear non-competitive inhibition between glyoxylate and 4,5-dioxovaleric acid (1.1-2.8 mM) was found. We show here that in vivo different enzymes exist for the transamination of glyoxylate and DOVA. |l eng | |
| 536 | |a Detalles de la financiación: National Council for Scientific Research | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: Maria Elisa Lombardo and Alcira M. del C. Batlle hold the post of Scientific Researchers in the Argentine National Research Council (CONICET). Lidi~: Susana Araujo is a Research Fellow of the University of Buenos Aires. This work was supported by grants from the CONICET. | ||
| 593 | |a Ctro. de Invest. Sobre P., Ciudad Universitaria Pab. II 2do., Piso - 1428, Buenos Aires, Argentina | ||
| 593 | |a Viamonte 1881, 10 A, CP-1056 Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a 5-AMINOLEVULINIC ACID BIOSYNTHESIS |
| 690 | 1 | 0 | |a EUGLENA GRACILIS |
| 690 | 1 | 0 | |a GLUTAMATE:4,5-DIOXOVALERATE TRASAMINASE |
| 690 | 1 | 0 | |a GLUTAMATE:GLYOXYLATE TRANSAMINASE |
| 690 | 1 | 0 | |a AMINOTRANSFERASE |
| 690 | 1 | 0 | |a GLUTAMIC ACID |
| 690 | 1 | 0 | |a GLYCINE |
| 690 | 1 | 0 | |a GLYOXYLIC ACID |
| 690 | 1 | 0 | |a VALERIC ACID DERIVATIVE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a ENZYME INHIBITION |
| 690 | 1 | 0 | |a ENZYME KINETICS |
| 690 | 1 | 0 | |a ENZYME MECHANISM |
| 690 | 1 | 0 | |a ENZYME SUBSTRATE COMPLEX |
| 690 | 1 | 0 | |a EUGLENA GRACILIS |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a TRANSAMINATION |
| 700 | 1 | |a Araujo, L.S. | |
| 700 | 1 | |a Del C. Batlle, A.M. | |
| 773 | 0 | |d 1996 |g v. 36 |h pp. 241-244 |k n. 3 |p J. PHOTOCHEM. PHOTOBIOL. B BIOL. |x 10111344 |w (AR-BaUEN)CENRE-515 |t Journal of Photochemistry and Photobiology B: Biology | |
| 856 | 4 | 1 | |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030484653&doi=10.1016%2fS1011-1344%2896%2907387-3&partnerID=40&md5=65bb77cb751543d387fe79b0e433d8a6 |y Registro en Scopus |
| 856 | 4 | 0 | |u https://doi.org/10.1016/S1011-1344(96)07387-3 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_10111344_v36_n3_p241_Lombardo |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10111344_v36_n3_p241_Lombardo |y Registro en la Biblioteca Digital |
| 961 | |a paper_10111344_v36_n3_p241_Lombardo |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 999 | |c 64366 | ||