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2 , the primary sequence alignment between the pectate and pectin lyase subfamilies has been corrected
3 atively charged pectin to create an extensin pectate coacervate that may template further orderly dep
5 thogen Erwinia chrysanthemi and degrades the pectate component of plant cell walls in soft rot diseas
8 he pel gene from an Amycolata sp. encoding a pectate lyase (EC 4.2.2.2) was isolated by activity scre
9 winia carotovora secrete several isozymes of pectate lyase (Pel) by the out-encoded type II pathway.
10 es showing sequence homology to higher-plant pectate lyase (Pel) genes were isolated from ripening ba
12 ora subsp. carotovora produces extracellular pectate lyase (Pel), polygalacturonase (Peh), cellulase
13 tococca, a plant pathogen, has two inducible pectate lyase (PL) genes (pel) encoding PL that can help
14 erase (PME), pectin acetylesterase (PAE) and pectate lyase (PL) where all highly expressed and latex-
15 hat the production of extracellular enzymes (pectate lyase [Pel], polygalacturonase [Peh], cellulase
16 we report a gene for a cellulosomal subunit, pectate lyase A (PelA), lying downstream of the engY gen
18 el gene in S. lividans TK24 resulted in high pectate lyase activity in the culture supernatant, conco
23 el clone produced a recombinant protein with pectate lyase activity, demonstrating that this sequence
25 e show that two pectin modification genes, a pectate lyase and pectinesterase, are targets of both bH
28 mensional structure of a complex between the pectate lyase C (PelC) R218K mutant and a plant cell wal
30 n with the structure of Erwinia chrysanthemi pectate lyase C (PelC), the primary sequence alignment b
33 he first avirulence gene and determined that pectate lyase C possessed a novel structural motif, know
38 uronate lyases (OGLs; now also classified as pectate lyase family 22) are cytoplasmic enzymes found i
40 bserved between the cellular distribution of pectate lyase folding and the distinct metal coordinatio
41 harpins have C-terminal enzyme-like domains: pectate lyase for HopAK1 and lytic transglycosylase for
44 ere we identify a Lotus japonicus nodulation pectate lyase gene (LjNPL), which is induced in roots an
46 orial extracts and high expression levels of pectate lyase genes suggest that the parasite contribute
47 cc71) produces extracellular enzymes such as pectate lyase isozymes (Pels), cellulase (Cel), polygala
48 mutants displayed a significant reduction in pectate lyase production, a virulence factor of this bac
50 l reactive arginine, analogous to the pectin/pectate lyase reaction site, is accessible to the solven
52 that an arginine, which is invariant in the pectate lyase superfamily, is the amino acid that initia
53 ycolata pectate lyase clearly belongs to the pectate lyase superfamily, sharing all functional amino
54 hlI (gene for AHL synthase), pel-1 (gene for pectate lyase), or rsmB (gene for regulatory RNA that bi
57 ) for the bHLH transcription factors and the pectate lyase, but not for the pectinesterase, complemen
59 ta-helix as seen in the pectinolytic enzymes pectate lyase, pectin lyase, polygalacturonase and rhamn
61 FlhDC(-) mutant produces very low levels of pectate lyase, polygalacturonase, cellulase, protease, a
62 rate-binding clefts of polygalacturonase and pectate lyase, which bind and cleave the same substrate,
63 e in a glycosylphosphatidylinositol-anchored pectate lyase-like gene) exhibited a strong increase in
70 ough the action of pectin-methylesterase and pectate-lyase that possibly originated from a microbial
71 nd Erwinia carotovora secrete extra-cellular pectate lyases (Pels) using the type II or Out pathway.
73 nearly identical to that found in the pectin/pectate lyases from several plant pathogenic microorgani
74 e C-terminal region of HrpW is homologous to pectate lyases of a unique class, suggesting that HrpW m
75 l DNA libraries more than 40 novel microbial pectate lyases were discovered, and their enzymatic prop
76 rwinia chrysanthemi belonging to family 1 of pectate lyases, a putative cellulose-binding domain, a c
77 E. chrysanthemi that belongs to family 4 of pectate lyases, and a duplicated sequence (or dockerin)
78 xpressed in mature pollen, shows homology to pectate lyases, and is the putative homologue of the tom
80 ructure and function of Erwinia chrysanthemi pectate lysase C, a plant virulence factor, is reviewed
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