Literature summary for 3.2.1.15 extracted from

Argolo Santos Carvalho, H.; de Andrade Silva, E.M.; Carvalho Santos, S.; Micheli, F.
Polygalacturonases from Moniliophthora perniciosa are regulated by fermentable carbon sources and possible post-translational modifications (2013), Fungal Genet. Biol., 60, 110-121.

Search for more literature for 3.2.1.15

Cloned(Commentary)

Cloned (Comment)	Organism
isozyme MpPG2, DNA and amino acid sequence determination and analysis	Moniliophthora perniciosa

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
38530	-	x * 38530, about, sequence calculation	Moniliophthora perniciosa

Organism

Organism	UniProt	Comment	Textmining
Moniliophthora perniciosa	E2LXX6	genes MpPG1, MpPG2 and MpPG3. Isozymes MpPG1and MpPG3 corresponds to exo-polygalacturonases, EC 3.2.1.67, while isozyme MpPG2 corresponds to endo-polygalacturonase	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	isozyme MpPG2 contains two probable glycosylation sites	Moniliophthora perniciosa
additional information	isozyme MpPG2 contains one putative acetylation site and one putative SUMOylation site	Moniliophthora perniciosa
phosphoprotein	isozyme MpPG2 contains 18 putative phosphorylation sites (3 Thr, 14 Ser, 1 Tyr)	Moniliophthora perniciosa

Source Tissue

Source Tissue	Comment	Organism	Textmining
mycelium	the isozyme MpPG2 shows different expression pattern from exo-polygalacturonase isozymes, dependent on the medium composition, overview	Moniliophthora perniciosa	-

Subunits

Subunits	Comment	Organism
?	x * 38530, about, sequence calculation	Moniliophthora perniciosa

Synonyms

Synonyms	Comment	Organism
MpPG2	-	Moniliophthora perniciosa

pI Value

Organism	Comment	pI Value Maximum	pI Value
Moniliophthora perniciosa	sequence calculation	-	4.41

General Information

General Information	Comment	Organism
evolution	the isozyme sequence contains a conserved domain of glycosyl hydrolase family 28/polygalacturonases	Moniliophthora perniciosa
metabolism	isozyme protein-protein interaction network analysis, overview	Moniliophthora perniciosa
additional information	active site cleft residues are identified: D210 for MpPG2 as general acid catalyst, residues D190/D211, as general base catalyst, and residue H232 which is involved in the regeneration of the acid-base equilibrium of the catalytic aspartate	Moniliophthora perniciosa
physiological function	the isozyme expression is mainly regulated by fermentable carbon sources galactose and mannose	Moniliophthora perniciosa

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Release 2023.1 (January 2023)