CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
*
Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.

Polysaccharide Lyase Family 22

From CAZypedia
Revision as of 10:56, 5 September 2014 by Richard McLean (talk | contribs)
Jump to navigation Jump to search
Under construction icon-blue-48px.png

This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Polysaccharide Lyase Family PL22
3D Structure β-7 propeller
Mechanism β-elimination
Charge neutraliser manganese
Active site residues known
CAZy DB link
http://www.cazy.org/PL22.html


Substrate specificities

PL22 [1].

Kinetics and Mechanism

Catalytic Residues

Three-dimensional structures

Family Firsts

First catalytic activity
OGTE from Pectobacterium carotovorum ICPB EC153 (previously Erwinia carotovora).[2]
First catalytic base identification
YeOGL (YE1876) H242 from Yersinia enterocolitica subsp. enterocolitica 8081.[1]
First catalytic divalent cation identification
OGL (Dda3937_03686) from Dickeya Dadantii 3937 (previously Erwinia chrysanthemi 3937).[3].
First 3-D structure
VPA0088 from Vibrio parahaemolyticus RIMD 2210633. (PDB 3C5M)

References

  1. Abbott DW, Gilbert HJ, and Boraston AB. (2010). The active site of oligogalacturonate lyase provides unique insights into cytoplasmic oligogalacturonate beta-elimination. J Biol Chem. 2010;285(50):39029-38. DOI:10.1074/jbc.M110.153981 | PubMed ID:20851883 [Abbott2010]
  2. Moran F, Nasuno S, and Starr MP. (1968). Oligogalacturonide trans-eliminase of Erwinia carotovora. Arch Biochem Biophys. 1968;125(3):734-41. DOI:10.1016/0003-9861(68)90508-0 | PubMed ID:5671040 [Moran1968]
  3. Shevchik VE, Condemine G, Robert-Baudouy J, and Hugouvieux-Cotte-Pattat N. (1999). The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J Bacteriol. 1999;181(13):3912-9. DOI:10.1128/JB.181.13.3912-3919.1999 | PubMed ID:10383957 [Shevchik1989]
  4. Collmer A and Bateman DF. (1981). Impaired induction and self-catabolite repression of extracellular pectate lyase in Erwinia chrysanthemi mutants deficient in oligogalacturonide lyase. Proc Natl Acad Sci U S A. 1981;78(6):3920-4. DOI:10.1073/pnas.78.6.3920 | PubMed ID:16593039 [Collmer1981]
  5. Kester HC, Magaud D, Roy C, Anker D, Doutheau A, Shevchik V, Hugouvieux-Cotte-Pattat N, Benen JA, and Visser J. (1999). Performance of selected microbial pectinases on synthetic monomethyl-esterified di- and trigalacturonates. J Biol Chem. 1999;274(52):37053-9. DOI:10.1074/jbc.274.52.37053 | PubMed ID:10601263 [Kester1999]
  6. Reverchon S and Robert-Baudouy J. (1987). Molecular cloning of an Erwinia chrysanthemi oligogalacturonate lyase gene involved in pectin degradation. Gene. 1987;55(1):125-33. DOI:10.1016/0378-1119(87)90255-1 | PubMed ID:3623103 [Reverchon1987]
  7. Reverchon S, Huang Y, Bourson C, and Robert-Baudouy J. (1989). Nucleotide sequences of the Erwinia chrysanthemi ogl and pelE genes negatively regulated by the kdgR gene product. Gene. 1989;85(1):125-34. DOI:10.1016/0378-1119(89)90472-1 | PubMed ID:2695393 [Reverchon1989]
  8. Yang S, Zhang Q, Guo J, Charkowski AO, Glick BR, Ibekwe AM, Cooksey DA, and Yang CH. (2007). Global effect of indole-3-acetic acid biosynthesis on multiple virulence factors of Erwinia chrysanthemi 3937. Appl Environ Microbiol. 2007;73(4):1079-88. DOI:10.1128/AEM.01770-06 | PubMed ID:17189441 [Yang2007]

All Medline abstracts: PubMed