@article {2645,
	title = {Composition of the epicuticular and intracuticular wax layers on Kalanchoe daigremontiana (Hamet et Perr. de la Bathie) leaves},
	journal = {Phytochemistry},
	volume = {70},
	number = {7},
	year = {2009},
	note = {ISI Document Delivery No.: 475UKTimes Cited: 1Cited Reference Count: 26van Maarseveen, Clare Jetter, Reinhard},
	month = {May},
	pages = {899-906},
	type = {Article},
	abstract = {Epicuticular and intracuticular waxes from both adaxial and abaxial surfaces of the leaves of Kalanchoe daigremontiana were analyzed. All wax mixtures were found to contain approximately equal amounts of triterpenoids and very long chain fatty acid (VLCFA) derivatives. The triterpenoid fraction consisted of glutinol (8-19\% of the total wax) and friedelin (4-9\%), together with smaller amounts of glutanol, glutinol acetate, epifriedelanol, germanicol and beta-amyrin. The VLCFA derivatives comprised C-27-C-35 alkanes (19-37\% of the total wax), C-32-C-34 aldehydes (3-7\%), C-32 and C-34 fatty acids (0.2-3\%), C-26-C-36 primary alcohols (4-8\%), and C-42-C-52 alkyl esters (2-9\%). The wax layers were found to differ in triterpenoid amounts, with the intracuticular wax containing higher percentages of most triterpenoids than the epicuticular wax. Friedelin, the only triterpenoid ketone present, showed the opposite distribution with higher proportions in the epicuticular wax. VLCFA derivatives also accumulated to higher percentages in the epicuticular than in the intracuticular wax layer. Epicuticular wax crystals were observed on both the adaxial and abaxial leaf surfaces. (C) 2009 Elsevier Ltd. All rights reserved.},
	keywords = {chain length, CHEMICAL-COMPOSITION, Crassulaceae, DUDLEYA, friedelin, glutinol, Kalanchoe daigremontiana, LEAF CUTICULAR WAXES, leaf surface, PINNATA, PLANTS, STEROLS, SURFACES, SYNTHASE, triterpenoids, Very long chain fatty acids},
	isbn = {0031-9422},
	url = {<Go to ISI>://000268386700009},
	author = {van Maarseveen, C. and Jetter, R.}
}
@article {1464,
	title = {PseG of pseudaminic acid biosynthesis - A UDP-sugar hydrolase as a masked glycosyltransferase},
	journal = {Journal of Biological Chemistry},
	volume = {281},
	number = {30},
	year = {2006},
	note = {ISI Document Delivery No.: 065VFTimes Cited: 12Cited Reference Count: 40Liu, Feng Tanner, Martin E.},
	month = {Jul},
	pages = {20902-20909},
	type = {Article},
	abstract = {The flagellin proteins in pathogenic bacteria such as Campylobacter jejuni and Helicobacter pylori are heavily glycosylated with the nine-carbon alpha-keto acid, pseudaminic acid. The presence of this posttranslational modification is absolutely required for assembly of functional flagella. Since motility is required for colonization, pseudaminic acid biosynthesis represents a virulence factor in these bacteria. Pseudaminic acid is generated from UDP-N-acetylglucosamine in five biosynthetic steps. The final step has been shown to involve the condensation of 2,4-diacetamido- 2,4,6-trideoxy-L-altrose ( 6-deoxy-AltdiNAc) with phosphoenolpyruvate as catalyzed by the enzyme pseudaminic acid synthase, NeuB3. The 6-deoxy-AltdiNAc used in this process is generated from its nucleotide-linked form, UDP-6-deoxy-AltdiNAc, by the action of a hydrolase that cleaves the glycosidic bond and releases UDP. This manuscript describes the first characterization of a UDP-6-deoxy-AltdiNAc hydrolase, namely PseG ( Cj1312) from C. jejuni. The activity of this enzyme is independent of the presence of divalent metal ions, and the values of the catalytic constants were found to be k(cat) = 27 s(-1) and K-m = 174 mu M. The enzyme was shown to hydrolyze the substrate with an overall inversion of stereochemistry at C-1 and to utilize a C-O bond cleavage mechanism during catalysis. These results, coupled with homology comparisons, suggest that the closest ancestors to the hydrolase are members of the metal-independent GT-B family of glycosyltransferases that include the enzyme MurG.},
	keywords = {CAMPYLOBACTER-JEJUNI, FLAGELLIN, FUNCTIONAL-CHARACTERIZATION, GLYCOPROTEINS, glycosylation, HELICOBACTER-PYLORI, IDENTIFICATION, MECHANISM, N-ACETYLGLUCOSAMINE 2-EPIMERASE, NUDIX HYDROLASES, SYNTHASE},
	isbn = {0021-9258},
	url = {<Go to ISI>://000239187300027},
	author = {Liu, F. and Tanner, M. E.}
}
@article {932,
	title = {Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1},
	journal = {Journal of Biological Chemistry},
	volume = {279},
	number = {47},
	year = {2004},
	note = {ISI Document Delivery No.: 870ZPTimes Cited: 14Cited Reference Count: 46},
	month = {Nov},
	pages = {49131-49137},
	type = {Article},
	abstract = {Although sumoylation regulates a diverse and growing number of recognized biological processes, the molecular mechanisms by which the covalent attachment of the ubiquitin-like protein SUMO can alter the properties of a target protein remain to be established. To address this question, we have used NMR spectroscopy to characterize the complex of mature SUMO-1 with the C-terminal domain of human RanGAP1. Based on amide chemical shift and N-15 relaxation measurements, we show that the C terminus of SUMO-1 and the loop containing the consensus sumoylation site in RanGAP1 are both conformationally flexible. Furthermore, the overall structure and backbone dynamics of each protein remain unchanged upon the covalent linkage of Lys(524) in RanGAP1 to the C-terminal Gly(97) of SUMO-1. Therefore, SUMO-1 and RanGAP1 behave as "beads-on-a-string," connected by a flexible isopeptide tether. Accordingly, the sumoylation-dependent interaction of RanGAP1 with the nucleoporin RanBP2 may arise through the bipartite recognition of both RanGAP1 and SUMO-1 rather than through a new binding surface induced in either individual protein upon their covalent linkage. We hypothesize that this conformational flexibility may be a general feature contributing to the recognition of ubiquitin-like modified proteins by their downstream effector machineries.},
	keywords = {BACKBONE DYNAMICS, BINDING, CONJUGATION, CRYSTAL-STRUCTURE, GTPASE-ACTIVATING PROTEIN, IN-VIVO, MOLYBDOPTERIN, NUCLEAR-PORE COMPLEX, SYNTHASE, UBC9, UBIQUITIN},
	isbn = {0021-9258},
	url = {<Go to ISI>://000225098100078},
	author = {Macauley, M. S. and Errington, W. J. and Okon, M. and Scharpf, M. and Mackereth, C. D. and Schulman, B. A. and McIntosh, L. P.}
}
