Literature summary for 3.1.1.11 extracted from

Habrylo, O.; Evangelista, D.E.; Castilho, P.V.; Pelloux, J.; Henrique-Silva, F.
The pectinases from Sphenophorus levis Potential for biotechnological applications (2018), Int. J. Biol. Macromol., 112, 499-508 .

Search for more literature for 3.1.1.11

Application

Application	Comment	Organism
food industry	the enzyme is suitable for both acidic and alkaline processing, such as coffee and tea fermentation	Sphenophorus levis

Cloned(Commentary)

Cloned (Comment)	Organism
sequence comparisons, the Sl-pectinase ORF, excluding the coding sequence for signal peptide, is cloned in frame with His-tag into pPICZalphaA and pPICZalphaB expression vectors, recombinant overexpression in Pichia pastoris strain KM71H	Sphenophorus levis

Inhibitors

Inhibitors	Comment	Organism	Structure
(-)-epigallocatechin gallate	exhibits 97.8% inhibition at 1 mg/ml and 47.0% at 0.1 mg/ml	Sphenophorus levis
additional information	no inhibition by PME inhibitor from kiwi fruits	Sphenophorus levis
NaCl	NaCl causes loss of 40% and 90% of enzyme activity at 0.1 M and 0.5 M, respectively	Sphenophorus levis
polyphenon 60	PP60, exhibits 94.8% inhibition at 1 mg/ml and 26.8% at 0.1 mg/ml	Sphenophorus levis
Tannic acid	exhibits 99.5% inhibition at 1 mg/ml and 55.2% at 0.1 mg/ml	Sphenophorus levis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Sphenophorus levis	-	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pectin + n H2O	Sphenophorus levis	-	n methanol + pectate	-	?

Organism

Organism	UniProt	Comment	Textmining
Sphenophorus levis	V9Q624	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	enzyme PME contains one N-glycosylation site, deglycosylation of Sl-pectinases is performed using endoglycosidase H (Endo H), peptide-N-glycosidase F (PNGase F) and O-glycosidase at 37°C	Sphenophorus levis

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from pastoris strain KM71H by nickel affinity chromatography	Sphenophorus levis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme is active on pectin substrates with degree of methylesterification (DM): sugar beet pectin (DM 42%) apple pectin (DM 70-75%), and citrus pectin (DM 20-34%, 55-70%, and over 85%), but not on polygalacturonic acid	Sphenophorus levis	?	-	?
pectin + n H2O	-	Sphenophorus levis	n methanol + pectate	-	?
pectin + n H2O	enzyme Sl-PME shows 100% of relative activity for 85% DM pectin, 51.1% for 55-70% DM pectin, 22.4% for 42% DM pectin and only 6.6% for 20-34% DM pectin	Sphenophorus levis	n methanol + pectate	-	?

Subunits

Subunits	Comment	Organism
?	x * 50000, about, recombinant His-tagged enzyme, SDS-PAGE	Sphenophorus levis

Synonyms

Synonyms	Comment	Organism
pectin methylesterase	-	Sphenophorus levis
Sl-PME	-	Sphenophorus levis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
40	-	recombinant enzyme	Sphenophorus levis

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
5	55	over 50% of maximal activity at 20-50°C, activity range, profile overview	Sphenophorus levis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
5	45	enzyme Sl-PME remains stable up to 35°C, activity decreases by 25% at 40°C and is completely abolished at 45°C	Sphenophorus levis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	recombinant enzyme	Sphenophorus levis

pH Range

pH Minimum	pH Maximum	Comment	Organism
6	9	inactive at pH 5.0 and above pH 10.0, over 90% of maximal activity at pH 6.0-8.0	Sphenophorus levis

General Information

General Information	Comment	Organism
physiological function	plant and bacterial pectin methylesterases (PMEs) perform the catalysis with a processive catalytic mechanism, unlike fungal PME whose activity leads to a random repartition of non-esterified carboxyl groups	Sphenophorus levis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)