Pectate trisaccharide-lyase: Difference between revisions

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Pectate trisaccharide-lyase
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]

^ 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[edit]

Pectate+trisaccharide-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[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.

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@@ Line 1: / Line 1: @@
 {{Infobox enzyme
-| Name = Pectate trisaccharide-lyase
+| Name       = Pectate trisaccharide-lyase
-| EC_number = 4.2.2.22
+| EC_number  = 4.2.2.22
 | CAS_number =
+| GO_code    =
-| IUBMB_EC_number = 4/2/2/22
-| GO_code =
+| image      =
-| image =
+| width      =
-| width =
+| caption    =
-| caption =
 }}
-'''Pectate trisaccharide-lyase''' ({{EC number|4.2.2.22}}, ''exopectate-lyase'', ''pectate lyase A'', ''PelA'') is an [[enzyme]] with system 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}}</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}}</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}}</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]]
 The predominant action of this enzyme is removal of a [[trisaccharide]].
 == References ==
@@ Line 20: / Line 19: @@
 == External links ==
 * {{MeshName|Pectate+trisaccharide-lyase}}
+{{Carbon-oxygen lyases}}
+{{Enzymes}}
+{{Portal bar|Biology|border=no}}
 [[Category:EC 4.2.2]]

v t e Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase
4.2.2: Acting on polysaccharides	Hyaluronate lyase Pectin lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)