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Polysaccharide Lyase Family 22
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|Polysaccharide Lyase Family PL22|
|3D Structure||β7 propeller|
|Active site residues||known|
|CAZy DB link|
Family 22 Polysaccharide Lyases (PL22s) contain two subfamilies and several outlier sequences . Originally known as oligogalacturonide transeliminases (OGTE) , PL22s are now commonly referred to as oligogalacturonide lyases (OGLs). This enzyme family is found primarily in phytopathogenic or intestinal bacteria where it plays a role in the metabolism of pectin.
PL22s remove 5-keto-4-deoxyuronate (4-deoxy-l-threo-5-hexosulose uronic acid, DKI) from short chain oligalacturonides and display preferential activity on digalacturonate and Δ4,5-unsaturated digalacturonate [3, 4]. Activity on trigalacturonate is significantly lower and PL22s appear to completely lack activity on long chain polymers of α-(1,4)-linked polygalacturonate [3, 4]. Differing levels of activity has been reported on methylated short chain oligogalacturonides depending on the location of methylation .
Kinetics and Mechanism
PL22s harness a β-elimination mechanism to cleave the glycosidic bonds in oligogalacturonides. This process requires a Brønstead base for proton abstraction and a catalytic metal (e.g. Mn2+ or Mg2+) for acidification of the α-proton and charge neutralization of the oxyanion intermediate. YePL22 (YE1876 from Yersinia enterocolitica subsp. enterocolitica 8081; gi|123442156|) displays the lowest reported pH optimum for a pectate lyase (7.3 - 7.7) , which is substantially lower than other families that deploy catalytic arginines or lysines in the β-elimination of pectate.
Within the structure of YePL22, H242 is the only basic residue that is in proximity to the α-proton of a modelled galacturonate . This histidine is highly conserved within PL22s with only Candidatus Solibacter usitatus Ellin6076 (gi|116225114|) displaying an alternative residue (T236); however, whether this protein is a lyase has yet to be determined. The 'stabilizing arginine'  (YE1876: R217) is completely conserved across the PL22 family.
The metal coordination pocket houses a manganese ion and is comprised of three histidines (VPA0088: H287, H353, H355; YE1876: H287, H353, H355) and one glutamine (VPA0088: Q350; YeOGL: Q350). It is of note however that although these residues are perfectly conserved in all reported subfamily 1 sequences and several outlier sequences, there are minor differences in subfamily 2 : H287 is invariant, Q350 is not conserved, and H353 and H355 have been replaced with a glutamate and asparagine respectively. These modifications may alter the chemistry of metal coordination selectivity. Further experimentation will be required to define this relationship.
Three-dimensional structuresPDB 3C5M) in 2008 by x-ray diffraction to 2.60 Å (Northeast Structural Genomics Consortium). This was followed in 2010 by YePL2A from Yersinia enterocolitica subsp. enterocolitica 8081 (PDB 3PE7), which was solved in complex with Mn2+ and acetate by x-ray diffraction to 1.65 Å . The two proteins share ~69% sequence identity and highly similar 3D structures. The PL22 fold is a β7 propeller with the catalytic machinery and metal coordination pocket housed at the center of the enzyme.
- First catalytic activity
- OGTE from Pectobacterium carotovorum ICPB EC153 (previously Erwinia carotovora) .
- First catalytic base identification
- YeOGL (YE1876) H242 from Yersinia enterocolitica subsp. enterocolitica 8081 .
- First catalytic divalent cation identification
- OGL (Dda3937_03686) from Dickeya Dadantii 3937 (previously Erwinia chrysanthemi 3937) .
- First 3-D structure
- VPA0088 from Vibrio parahaemolyticus RIMD 2210633 (Unpublished: PDB 3C5M).
- Lombard V, Bernard T, Rancurel C, Brumer H, Coutinho PM, and Henrissat B. (2010) A hierarchical classification of polysaccharide lyases for glycogenomics. Biochem J. 432, 437-44. DOI:10.1042/BJ20101185 |
- Moran F, Nasuno S, and Starr MP. (1968) Oligogalacturonide trans-eliminase of Erwinia carotovora. Arch Biochem Biophys. 125, 734-41.
- 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. 285, 39029-38. DOI:10.1074/jbc.M110.153981 |
- 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. 274, 37053-9.
- 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. 181, 3912-9.
- 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. 78, 3920-4.
- Reverchon S and Robert-Baudouy J. (1987) Molecular cloning of an Erwinia chrysanthemi oligogalacturonate lyase gene involved in pectin degradation. Gene. 55, 125-33.
- 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. 85, 125-34.
- 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. 73, 1079-88. DOI:10.1128/AEM.01770-06 |