Pectate trisaccharide-lyase: Difference between revisions
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'''Pectate trisaccharide-lyase''' ({{ |
'''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]]: |
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: eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of [[polygalacturonic acid]]/[[pectate]] |
: eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of [[polygalacturonic acid]]/[[pectate]] |
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Revision as of 14:48, 29 July 2022
| Pectate trisaccharide-lyase | |||||||||
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| Identifiers | |||||||||
| EC no. | 4.2.2.22 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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
- ^ 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.
- ^ 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.
- ^ 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
- Pectate+trisaccharide-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
