EC |
3.2.1.15 |
Accepted name: |
endo-polygalacturonase |
Reaction: |
(1,4-α-D-galacturonosyl)n+m + H2O = (1,4-α-D-galacturonosyl)n + (1,4-α-D-galacturonosyl)m |
Other name(s): |
pectin depolymerase (ambiguous); pectinase (ambiguous); endopolygalacturonase; pectolase (ambiguous); pectin hydrolase (ambiguous); pectin polygalacturonase (ambiguous); polygalacturonase (ambiguous); poly-α-1,4-galacturonide glycanohydrolase (ambiguous); endogalacturonase; endo-D-galacturonase; poly(1,4-α-D-galacturonide) glycanohydrolase (ambiguous) |
Systematic name: |
(1→4)-α-D-galacturonan glycanohydrolase (endo-cleaving) |
Comments: |
The enzyme catalyses the random hydrolysis of (1→4)-α-D-galactosiduronic linkages in pectate and other galacturonans. Different forms of the enzyme have different tolerances to methyl esterification of the substrate. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9032-75-1 |
References: |
1. |
Lineweaver, H. and Jansen, E.F. Pectic enzymes. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 267–295. |
2. |
McCready, R.M. and Seegmiller, C.G. Action of pectic enzymes on oligogalacturonic acids and some of their derivatives. Arch. Biochem. Biophys. 50 (1954) 440–450. [DOI] [PMID: 13159344] |
3. |
Phaff, H.J. and Demain, A.L. The unienzymatic nature of yeast polygalacturonase. J. Biol. Chem. 218 (1956) 875–884. [PMID: 13295238] |
4. |
Deuel, H. and Stutz, E. Pectic substances and pectic enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 20 (1958) 341–382. [PMID: 13605988] |
5. |
Mill, P.J. and Tuttobello, R. The pectic enzymes of Aspergillus niger. 2. Endopolygalacturonase. Biochem. J. 79 (1961) 57–64. [PMID: 13770689] |
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[EC 3.2.1.15 created 1961, modified 2019] |
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