Identification of essential amino acids in the bacterial α-mannosyltransferase AceA
The α-mannosyltransferase AceA from Acetobacter xylinum belongs to the CaZY family 4 of retaining glycosyltransferases. We have identified a series of either highly conserved or invariant residues that are found in all family 4 enzymes as well as other retaining glycosyltransferases. These residues...
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| Formato: | Capítulo de libro |
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2000
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| LEADER | 08326caa a22011177a 4500 | ||
|---|---|---|---|
| 001 | PAPER-2124 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203131.0 | ||
| 008 | 190411s2000 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0034704103 | |
| 024 | 7 | |2 cas |a Amino Acids, Essential; GDP-mannose - cellobiosyl-diphosphopolyprenol mannosyltransferase, EC 2.4.1.-; Mannosyltransferases, EC 2.4.1.-; Recombinant Proteins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a JBCHA | ||
| 100 | 1 | |a Abdian, P.L. | |
| 245 | 1 | 0 | |a Identification of essential amino acids in the bacterial α-mannosyltransferase AceA |
| 260 | |c 2000 | ||
| 270 | 1 | 0 | |m Geremia, R.A.; CERMAV/CNRS, BP 53, 38041 Grenoble Cedex 9, France; email: roberto.geremia@cermav.cnrs.fr |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a The α-mannosyltransferase AceA from Acetobacter xylinum belongs to the CaZY family 4 of retaining glycosyltransferases. We have identified a series of either highly conserved or invariant residues that are found in all family 4 enzymes as well as other retaining glycosyltransferases. These residues included Glu-287 and Glu-295, which comprise an EX7E motif and have been proposed to be involved in catalysis. Alanine replacements of each conserved residue were constructed by site-directed mutagenesis. The mannosyltransferase activity of each mutant was examined by both an in vitro transferase assay using recombinant mutant AceA expressed in Escherichia coli and by an in vivo rescue assay by expressing the mutant AceA in a Xanthomonas campestris gumH- strain. We found that only mutants K211A and E287A lost all detectable activity both in vitro and in vivo, whereas E295A retained residual activity in the more sensitive in vivo assay. H127A and S162A each retained reduced but significant activities both in vitro and in vivo. Secondary structure predictions of AceA and subsequent comparison with the crystal structures of the T4 β-glucosyltransferase and MurG suggest that AceA Lys-211 and Glu-295 are involved in nucleotide sugar donor binding, leaving Glu-287 of the EX7E as a potential catalytic residue. |l eng | |
| 593 | |a Instituto de Investigaciones Bioquímicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Consejo Nacional de Investigaciones Científicas y Técnicas, Avenida Patricias Argentinas 435, 1045 Buenos Aires, Argentina | ||
| 593 | |a Centre de Recherches Sur Les Macromolécules Végétales, CNRS, Joseph Fourier University, BP 53X, 38041 Grenoble Cedex 9, France | ||
| 593 | |a CERMAV/CNRS, BP 53, 38041 Grenoble Cedex 9, France | ||
| 593 | |a Carrera del Investigador, Consejo Nacional de Investigaciones CientIficas y Técnicas, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ALPHA MANNOSYLTRANSFERASE ACEA |
| 690 | 1 | 0 | |a BACTERIAL ENZYME |
| 690 | 1 | 0 | |a ESSENTIAL AMINO ACID |
| 690 | 1 | 0 | |a GLUCOSYLTRANSFERASE |
| 690 | 1 | 0 | |a MANNOSYLTRANSFERASE |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a ACETOBACTER |
| 690 | 1 | 0 | |a AMINO ACID SUBSTITUTION |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CELLULAR DISTRIBUTION |
| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a ENZYME ANALYSIS |
| 690 | 1 | 0 | |a ENZYME STRUCTURE |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a STRUCTURE ANALYSIS |
| 690 | 1 | 0 | |a ACETOBACTER |
| 690 | 1 | 0 | |a AMINO ACIDS, ESSENTIAL |
| 690 | 1 | 0 | |a CATALYSIS |
| 690 | 1 | 0 | |a MANNOSYLTRANSFERASES |
| 690 | 1 | 0 | |a NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE, SECONDARY |
| 690 | 1 | 0 | |a RECOMBINANT PROTEINS |
| 690 | 1 | 0 | |a ACETOBACTER |
| 690 | 1 | 0 | |a BACTERIA (MICROORGANISMS) |
| 690 | 1 | 0 | |a ESCHERICHIA COLI |
| 690 | 1 | 0 | |a GLUCONACETOBACTER XYLINUS |
| 690 | 1 | 0 | |a XANTHOMONAS CAMPESTRIS |
| 700 | 1 | |a Lellouch, A.C. | |
| 700 | 1 | |a Gautier, C. | |
| 700 | 1 | |a Ielpi, L. | |
| 700 | 1 | |a Geremia, R.A. | |
| 773 | 0 | |d 2000 |g v. 275 |h pp. 40568-40575 |k n. 51 |p J. Biol. Chem. |x 00219258 |w (AR-BaUEN)CENRE-175 |t Journal of Biological Chemistry | |
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| 856 | 4 | 0 | |u https://doi.org/10.1074/jbc.M007496200 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_00219258_v275_n51_p40568_Abdian |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v275_n51_p40568_Abdian |y Registro en la Biblioteca Digital |
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| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 963 | |a NORI | ||
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