Pectate trisaccharide-lyase: Difference between revisions
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'''Pectate trisaccharide-lyase''' ({{EC number|4.2.2.22}}, ''exopectate-lyase'', ''pectate lyase A'', ''PelA'') is an [[enzyme]] with |
'''Pectate trisaccharide-lyase''' ({{EC number|4.2.2.22}}, ''exopectate-lyase'', ''pectate lyase A'', ''PelA'') is an [[enzyme]] with systematic name ''(1->4)-alpha-D-galacturonan reducing-end-trisaccharide-lyase''.<ref>{{cite journal | title = Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium <em>Thermotoga maritima</em> |author = Kluskens, L.D., van Alebeek, G.J., Voragen, A.G., de Vos, W.M. and van der Oost, J. |journal = Biochem. J. |date = 2003 |volume = 370 |pages = 651-659 |pmid = 12443532 |doi=10.1042/bj20021595}}</ref><ref>{{cite journal | title = Pectate lyase A, an enzymatic subunit of the <em>Clostridium cellulovorans</em> cellulosome |author = Tamaru, Y. and Doi, R.H. |journal = Proc. Natl. Acad. Sci. USA |date = 2001 |volume = 98 |pages = 4125-4129 |pmid = 11259664 |doi=10.1073/pnas.071045598}}</ref><ref>{{cite journal | title = Cloning of the <em>pelA</em> gene from <em>Bacillus licheniformis</em> 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase |author = Berensmeier, S., Singh, S.A., Meens, J. and Buchholz, K. |journal = Appl. Microbiol. Biotechnol. |date = 2004 |volume = 64 |pages = 560-567 |pmid = 14673544 |doi=10.1007/s00253-003-1446-9}}</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]] |
Revision as of 18:30, 30 March 2016
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)-alpha-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, L.D., van Alebeek, G.J., Voragen, A.G., de Vos, W.M. and van der Oost, J. (2003). "Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima". Biochem. J. 370: 651–659. doi:10.1042/bj20021595. PMID 12443532.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ Tamaru, Y. and Doi, R.H. (2001). "Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome". Proc. Natl. Acad. Sci. USA. 98: 4125–4129. doi:10.1073/pnas.071045598. PMID 11259664.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ Berensmeier, S., Singh, S.A., Meens, J. and Buchholz, K. (2004). "Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase". Appl. Microbiol. Biotechnol. 64: 560–567. doi:10.1007/s00253-003-1446-9. PMID 14673544.
{{cite journal}}
: CS1 maint: multiple names: authors list (link)
External links
- Pectate+trisaccharide-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)