ライフサイエンスコーパス: pectate lyase

1 alin A), and parallel beta-helical proteins (pectate lyase).

2 of ripening, by silencing a gene encoding a pectate lyase.

3 e active site and substrate-binding cleft of pectate lyase.

4 combined activities of polygalacturonase and pectate lyase.

5 e distinct metal coordination chemistries of pectate lyases.

6 we report a gene for a cellulosomal subunit, pectate lyase A (PelA), lying downstream of the engY gen

7 One of these cDNAs shows homology to pectate lyase, a pectin-degrading enzyme.

8 rwinia chrysanthemi belonging to family 1 of pectate lyases, a putative cellulose-binding domain, a c

9 a significant increase in calcium-dependent pectate lyase activity during ripening.

10 el gene in S. lividans TK24 resulted in high pectate lyase activity in the culture supernatant, conco

11 Pectate lyase activity is detected in elongating and dif

12 No pectate lyase activity was detected in E. coli BL21 with

13 Although no pectate lyase activity was detected, the C-terminal regi

14 The purified LjNPL protein had pectate lyase activity, demonstrating that this activity

15 el clone produced a recombinant protein with pectate lyase activity, demonstrating that this sequence

16 Escherichia coli possesses calcium-dependent pectate lyase activity.

17 e show that two pectin modification genes, a pectate lyase and pectinesterase, are targets of both bH

18 E. chrysanthemi that belongs to family 4 of pectate lyases, and a duplicated sequence (or dockerin)

19 xpressed in mature pollen, shows homology to pectate lyases, and is the putative homologue of the tom

20 ) for the bHLH transcription factors and the pectate lyase, but not for the pectinesterase, complemen

21 The folding mechanism of pectate lyase C (pelC) involves two slow phases that hav

22 Pectate lyase C (pelC) is a member of the class of prote

23 mensional structure of a complex between the pectate lyase C (PelC) R218K mutant and a plant cell wal

24 Pectate lyase C (pelC) was the first protein in which th

25 n with the structure of Erwinia chrysanthemi pectate lyase C (PelC), the primary sequence alignment b

26 or in vitro activity of Erwinia chrysanthemi pectate lyase C (PelC).

27 When modeled based on pectate lyase C of Erwinia chrysanthemi, the RHbetaH of

28 he first avirulence gene and determined that pectate lyase C possessed a novel structural motif, know

29 gh levels of the exoenzyme virulence factors pectate lyase, cellulase and protease.

30 The Amycolata pectate lyase clearly belongs to the pectate lyase super

31 The Amycolata pectate lyase contains a signal peptide of 26 amino acid

32 he pel gene from an Amycolata sp. encoding a pectate lyase (EC 4.2.2.2) was isolated by activity scre

33 ase family, in contrast to that found in the pectate lyase enzymes.

34 High xylanase or pectate lyase expression was observed when C. cellulovor

35 uronate lyases (OGLs; now also classified as pectate lyase family 22) are cytoplasmic enzymes found i

36 e invariant and conserved amino acids in the pectate lyase family of proteins.

37 bserved between the cellular distribution of pectate lyase folding and the distinct metal coordinatio

38 harpins have C-terminal enzyme-like domains: pectate lyase for HopAK1 and lytic transglycosylase for

39 with PelE from Erwinia chrysanthemi and the pectate lyase from Glomerella cingulata.

40 inal amino-acid sequence match the wild-type pectate lyase from the Amycolata sp.

41 nearly identical to that found in the pectin/pectate lyases from several plant pathogenic microorgani

42 ere we identify a Lotus japonicus nodulation pectate lyase gene (LjNPL), which is induced in roots an

43 re have been no reports available to date on pectate lyase genes from Clostridia.

44 orial extracts and high expression levels of pectate lyase genes suggest that the parasite contribute

45 cc71) produces extracellular enzymes such as pectate lyase isozymes (Pels), cellulase (Cel), polygala

46 e in a glycosylphosphatidylinositol-anchored pectate lyase-like gene) exhibited a strong increase in

47 a previously described member of a family of pectate lyase-like genes.

48 PMR6 encodes a pectate lyase-like protein with a novel C-terminal domai

49 re we report direct interaction of NPG1 with pectate lyase-like proteins (PLLs).

50 e C-terminal region of HrpW is homologous to pectate lyases of a unique class, suggesting that HrpW m

51 hlI (gene for AHL synthase), pel-1 (gene for pectate lyase), or rsmB (gene for regulatory RNA that bi

52 ta-helix as seen in the pectinolytic enzymes pectate lyase, pectin lyase, polygalacturonase and rhamn

53 winia carotovora secrete several isozymes of pectate lyase (Pel) by the out-encoded type II pathway.

54 es showing sequence homology to higher-plant pectate lyase (Pel) genes were isolated from ripening ba

55 uppress host defense responses, and secretes pectate lyase (Pel) to degrade the plant cell wall.

56 ora subsp. carotovora produces extracellular pectate lyase (Pel), polygalacturonase (Peh), cellulase

57 hat the production of extracellular enzymes (pectate lyase [Pel], polygalacturonase [Peh], cellulase

58 nd Erwinia carotovora secrete extra-cellular pectate lyases (Pels) using the type II or Out pathway.

59 protein with domains resembling harpins and pectate lyases (Pels), respectively.

60 tococca, a plant pathogen, has two inducible pectate lyase (PL) genes (pel) encoding PL that can help

61 erase (PME), pectin acetylesterase (PAE) and pectate lyase (PL) where all highly expressed and latex-

62 The basal levels of extracellular pectate lyase, polygalacturonase, and cellulase as well

63 FlhDC(-) mutant produces very low levels of pectate lyase, polygalacturonase, cellulase, protease, a

64 mutants displayed a significant reduction in pectate lyase production, a virulence factor of this bac

65 ng that this sequence was likely to encode a pectate lyase protein in planta.

66 l reactive arginine, analogous to the pectin/pectate lyase reaction site, is accessible to the solven

67 In contrast, PelE, a pectate lyase secreted via the type II protein secretion

68 that an arginine, which is invariant in the pectate lyase superfamily, is the amino acid that initia

69 ycolata pectate lyase clearly belongs to the pectate lyase superfamily, sharing all functional amino

70 ough the action of pectin-methylesterase and pectate-lyase that possibly originated from a microbial

71 l DNA libraries more than 40 novel microbial pectate lyases were discovered, and their enzymatic prop

72 rate-binding clefts of polygalacturonase and pectate lyase, which bind and cleave the same substrate,