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{{Infobox enzyme
{{Infobox enzyme
| Name = Pectate trisaccharide-lyase
| Name = Rhamnogalacturonan exolyase
| EC_number = 4.2.2.24
| EC_number = 4.2.2.22
| CAS_number =
| CAS_number =
| GO_code =
| IUBMB_EC_number = 4/2/2/24
| GO_code =
| image =
| image =
| width =
| width =
| caption =
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}}
}}
'''Rhamnogalacturonan exolyase''' ({{EC number|4.2.2.24}}, ''YesX'') is an [[enzyme]] with system name ''alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronate exolyase''.<ref>{{cite journal | title = Structural determinants responsible for substrate recognition and mode of action in family 11 polysaccharide lyases |author = Ochiai, A., Itoh, T., Mikami, B., Hashimoto, W. and Murata, K. |journal = J. Biol. Chem. |date = 2009 |volume = 284 |pages = 10181-10189 |pmid = 19193638}}</ref><ref>{{cite journal | title = Plant cell wall degradation by saprophytic <em>Bacillus subtilis</em> strains: gene clusters responsible for rhamnogalacturonan depolymerization |author = Ochiai, A., Itoh, T., Kawamata, A., Hashimoto, W. and Murata, K. |journal = Appl. Environ. Microbiol. |date = 2007 |volume = 73 |pages = 3803-3813 |pmid = 17449691}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
'''Pectate trisaccharide-lyase''' ({{EnzExplorer|4.2.2.22}}, ''exopectate-lyase'', ''pectate lyase A'', ''PelA'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''(1→4)-α-<small>D</small>-galacturonan reducing-end-trisaccharide-lyase''.<ref>{{cite journal | vauthors = Kluskens LD, van Alebeek GJ, Voragen AG, de Vos WM, van der Oost J | title = Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima | journal = The Biochemical Journal | volume = 370 | issue = Pt 2 | pages = 651–9 | date = March 2003 | pmid = 12443532 | pmc = 1223193 | doi = 10.1042/bj20021595 }}</ref><ref>{{cite journal | vauthors = Tamaru Y, Doi RH | title = Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 7 | pages = 4125–9 | date = March 2001 | pmid = 11259664 | pmc = 31190 | doi = 10.1073/pnas.071045598 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Berensmeier S, Singh SA, Meens J, Buchholz K | title = Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase | journal = Applied Microbiology and Biotechnology | volume = 64 | issue = 4 | pages = 560–7 | date = May 2004 | pmid = 14673544 | doi = 10.1007/s00253-003-1446-9 | s2cid = 23236787 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]:


: eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of [[polygalacturonic acid]]/[[pectate]]
: Exotype eliminative cleavage of alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosacharides containing alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.


The predominant action of this enzyme is removal of a [[trisaccharide]].
The enzyme is part of the degradation system for rhamnogalacturonan I in ''[[Bacillus subtilis]]'' strain 168.


== References ==
== References ==
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== External links ==
== External links ==
* {{MeshName|Rhamnogalacturonan+exolyase}}
* {{MeshName|Pectate+trisaccharide-lyase}}

{{Carbon-oxygen lyases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}


[[Category:EC 4.2.2]]
[[Category:EC 4.2.2]]

Latest revision as of 15:17, 26 August 2023

Pectate trisaccharide-lyase
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EC no.4.2.2.22
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Pectate trisaccharide-lyase (EC 4.2.2.22, exopectate-lyase, pectate lyase A, PelA) is an enzyme with systematic name (1→4)-α-D-galacturonan reducing-end-trisaccharide-lyase.[1][2][3] This enzyme catalyses the following chemical reaction:

eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate

The predominant action of this enzyme is removal of a trisaccharide.

References[edit]

  1. ^ Kluskens LD, van Alebeek GJ, Voragen AG, de Vos WM, van der Oost J (March 2003). "Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima". The Biochemical Journal. 370 (Pt 2): 651–9. doi:10.1042/bj20021595. PMC 1223193. PMID 12443532.
  2. ^ Tamaru Y, Doi RH (March 2001). "Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome". Proceedings of the National Academy of Sciences of the United States of America. 98 (7): 4125–9. doi:10.1073/pnas.071045598. PMC 31190. PMID 11259664.
  3. ^ Berensmeier S, Singh SA, Meens J, Buchholz K (May 2004). "Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase". Applied Microbiology and Biotechnology. 64 (4): 560–7. doi:10.1007/s00253-003-1446-9. PMID 14673544. S2CID 23236787.

External links[edit]

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