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InterPro: IPR000070 Pectinesterase, catalytic

Protein matchesHelp
UniProtKB
Matches:
1112 proteins
AccessionHelp IPR000070 Pectinesterase_cat
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR012334 Pectin lyase fold
Contains IPR018040 Pectinesterase, active site
GO Term annotationHelp
Process GO:0042545 cell wall modification
Function GO:0030599 pectinesterase activity
Component GO:0005618 cell wall
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Pectinesterase EC:3.1.1.11 (pectin methylesterase) catalyses the de-esterification of pectin into pectate and methanol. Pectin is one of the main components of the plant cell wall. In plants, pectinesterase plays an important role in cell wall metabolism during fruit ripening. In plant bacterial pathogens such as Erwinia carotovora and in fungal pathogens such as Aspergillus niger, pectinesterase is involved in maceration and soft-rotting of plant tissue. Plant pectinesterases are regulated by pectinesterase inhibitors, which are ineffective against microbial enzymes [1].

Prokaryotic and eukaryotic pectinesterases share a few regions of sequence similarity. The crystal structure of pectinesterase from Erwinia chrysanthemi revealed a beta-helix structure similar to that found in pectinolytic enzymes, though it is different from most structures of esterases [2]. The putative catalytic residues are in a similar location to those of the active site and substrate-binding cleft of pectate lyase.

Structural linksHelp
SCOP: b.80.1.5
CATH: 2.160.20.10
Database linksHelp
PDBe-motif: PS00503 , PS00800
Enzyme: EC:3.1.1.11
PROSITE doc: PDOC00413
PANDIT: PF01095
Blocks: IPB000070
Pfam Clan: CL0268.3

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000070 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O04953 Putative pectinesterase 52

P0C1A8 Pectinesterase A

P14280 Pectinesterase 1

P17872 Pectinesterase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR012334 Pectin lyase fold
IPR018040 Pectinesterase, active site
IPR000070 Pectinesterase, catalytic
IPR006501 Pectinesterase inhibitor
IPR011050 Pectin lyase fold/virulence factor
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D.
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein.
Plant Cell 17 849-58 2005 [PubMed: 15722470]
http://dx.doi.org/10.1105/tpc.104.028886
2. Jenkins J, Mayans O, Smith D, Worboys K, Pickersgill RW.
Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site.
J. Mol. Biol. 305 951-60 2001 [PubMed: 11162105]
http://dx.doi.org/10.1006/jmbi.2000.4324

Additional ReadingHelp
Giovane A, Servillo L, Balestrieri C, Raiola A, D'Avino R, Tamburrini M, Ciardiello MA, Camardella L.
Pectin methylesterase inhibitor.
Biochim. Biophys. Acta 1696 2004 245-52 [PubMed: 14871665]
Johansson K, El-Ahmad M, Friemann R, Jornvall H, Markovic O, Eklund H.
Crystal structure of plant pectin methylesterase.
FEBS Lett. 514 2002 243-9 [PubMed: 11943159]
http://dx.doi.org/10.1016/S0014-5793(02)02372-4
D'Avino R, Camardella L, Christensen TM, Giovane A, Servillo L.
Tomato pectin methylesterase: modeling, fluorescence, and inhibitor interaction studies-comparison with the bacterial (Erwinia chrysanthemi) enzyme.
Proteins 53 2003 830-9 [PubMed: 14635125]
http://dx.doi.org/10.1002/prot.10487
Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW.
Molecular basis of the activity of the phytopathogen pectin methylesterase.
EMBO J. 26 2007 3879-87 [PubMed: 17717531]
http://dx.doi.org/10.1038/sj.emboj.7601816
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InterPro 23.1