The active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis.
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The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharideStructural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implicationsStructural insights into the processivity of endopolygalacturonase I from Aspergillus nigerCrystal structure of endo-xylogalacturonan hydrolase from Aspergillus tubingensisActive site characterization of the single endo-polygalacturonase produced by Fusarium moniliforme NCIM 1276.The interaction between endopolygalacturonase from Fusarium moniliforme and PGIP from Phaseolus Vulgaris studied by surface plasmon resonance and mass spectrometry.Epimerase active domain of Pseudomonas aeruginosa AlgG, a protein that contains a right-handed beta-helix.Structure and function of pectic enzymes: virulence factors of plant pathogens.Molecular cloning and expression of three polygalacturonase cDNAs from the tarnished plant bug, Lygus lineolarisInsights into the Activity and Substrate Binding of Xylella fastidiosa Polygalacturonase by Modification of a Unique QMK Amino Acid Motif Using Protein Chimeras.Probing the role of cation-π interaction in the thermotolerance and catalytic performance of endo-polygalacturonases.Studying protein-carbohydrate interactions by amide hydrogen/deuterium exchange mass spectrometry.A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation.Study of the mode of action of a polygalacturonase from the phytopathogen Burkholderia cepacia.Identification of amino acid residues critical for catalysis and stability in Aspergillus niger family 1 pectin lyase A.Changing a single amino acid residue switches processive and non-processive behavior of Aspergillus niger endopolygalacturonase I and II.Cell wall-degrading enzymes enlarge the pore size of intervessel pit membranes in healthy and Xylella fastidiosa-infected grapevines.Tandemly duplicated Arabidopsis genes that encode polygalacturonase-inhibiting proteins are regulated coordinately by different signal transduction pathways in response to fungal infection.Targeted modification of homogalacturonan by transgenic expression of a fungal polygalacturonase alters plant growth.ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE1 (ADPG1), ADPG2, and QUARTET2 are Polygalacturonases required for cell separation during reproductive development in Arabidopsis.A critical survey of average distances between catalytic carboxyl groups in glycoside hydrolases.Subsite mapping of Aspergillus niger endopolygalacturonase II by site-directed mutagenesis.Fungal endopolygalacturonases are recognized as microbe-associated molecular patterns by the arabidopsis receptor-like protein RESPONSIVENESS TO BOTRYTIS POLYGALACTURONASES1.Elicitor activity of a fungal endopolygalacturonase in tobacco requires a functional catalytic site and cell wall localizationThe polygalacturonase-inhibiting protein PGIP2 of Phaseolus vulgaris has evolved a mixed mode of inhibition of endopolygalacturonase PG1 of Botrytis cinerea
P2860
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P2860
The active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
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2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
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2000年學術文章
@zh-hant
name
The active site topology of As ...... by site-directed mutagenesis.
@en
type
label
The active site topology of As ...... by site-directed mutagenesis.
@en
prefLabel
The active site topology of As ...... by site-directed mutagenesis.
@en
P2093
P2860
P356
P1476
The active site topology of As ...... by site-directed mutagenesis.
@en
P2093
Dijkstra BW
Sánchez-Torres P
Wagemaker MJ
van Santen Y
P2860
P304
P356
10.1074/JBC.275.1.691
P407
P577
2000-01-01T00:00:00Z