Enzymes
| UniProtKB help_outline | 1 proteins |
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| GO Molecular Function help_outline |
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Name help_outline
[(1→4)-α-D-galacturonosyl](n)
Identifier
CHEBI:140523
Charge
-1
Formula
(C6H7O6)n.H2O
Search links
Involved in 5 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:14570Polymer name: [(1→4)-α-D-galacturonosyl](n)Polymerization index help_outline nFormula H2O(C6H7O6)nCharge (0)(-1)nMol File for the polymer
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Identifier: RHEA-COMP:14734Polymer name: [(1→4)-α-D-galacturonosyl](n−2)Polymerization index help_outline n-2Formula H2O(C6H7O6)n-2Charge (0)(-1)n-2Mol File for the polymer
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-D-galacturonosyl-(1→4)-D-galacturonate Identifier CHEBI:141004 Charge -2 Formula C12H16O13 InChIKeyhelp_outline IGSYEZFZPOZFNC-LKIWRGPLSA-L SMILEShelp_outline [C@@H]1(O[C@@H]([C@@H]([C@@H]([C@H]1O)O)O)C(=O)[O-])O[C@H]2[C@H](OC([C@@H]([C@H]2O)O)O)C(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:56232 | RHEA:56233 | RHEA:56234 | RHEA:56235 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-alpha-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16.
He S.Y., Collmer A.
The pehX gene encoding extracellular exo-poly-alpha-D-galacturonosidase (exoPG; EC 3.2.1.82) was isolated from a genomic library of the pectate lyase-deficient Erwinia chrysanthemi mutant UM1005 (a Nalr Kanr delta pelABCE derivative of EC16) by immunoscreening 2,800 Escherichia coli HB101 transfor ... >> More
The pehX gene encoding extracellular exo-poly-alpha-D-galacturonosidase (exoPG; EC 3.2.1.82) was isolated from a genomic library of the pectate lyase-deficient Erwinia chrysanthemi mutant UM1005 (a Nalr Kanr delta pelABCE derivative of EC16) by immunoscreening 2,800 Escherichia coli HB101 transformants with an antibody against exoPG protein. The cloned pehX gene was expressed highly from its own promoter in E. coli, and most of the enzyme was localized in the periplasm. The nucleotide sequence of pehX revealed the presence of an amino-terminal signal peptide and an open reading frame encoding a preprotein of 64,608 daltons. The cloned pehX gene was insertionally inactivated with TnphoA and used to mutate the chromosomal pehX gene of E. chrysanthemi AC4150 (Nalr) and CUCPB5006 (Nalr Kans delta pelABCE) by marker exchange mutagenesis. Analysis of the resulting mutants, CUCPB5008 (Pel+ Peh-) and CUCPB5009 (Pel-Peh-), indicated that exoPG can contribute significantly to bacterial utilization of polygalacturonate and the induction of pectate lyase in the presence of extracellular pectic polymers. CUCPB5009 retained a slight ability to pit polygalacturonate semisolid agar and macerated chrysanthemum pith tissues when large numbers of bacteria were inoculated. << Less
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Isolation of an oligogalacturonate hydrolase from a Bacillus specie.
Hasegawa S., Nagel C.W.