Information on EC 3.1.1.86 - rhamnogalacturonan acetylesterase

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The expected taxonomic range for this enzyme is: Aspergillus aculeatus

EC NUMBER
COMMENTARY hide
3.1.1.86
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RECOMMENDED NAME
GeneOntology No.
rhamnogalacturonan acetylesterase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of alpha-D-galacturonic acid in rhamnogalacturonan I.
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
rhamnogalacturonan type I degradation I (fungi)
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SYSTEMATIC NAME
IUBMB Comments
rhamnogalacturonan 2/3-O-acetyl-alpha-D-galacturonate O-acetylhydrolase
The degradation of rhamnogalacturonan by rhamnogalacturonases depends on the removal of the acetyl esters from the substrate [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetylated rhamnogalacturonan I + H2O
acetate + deacetylated rhamnogalacturonan I
show the reaction diagram
additional information
?
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native and recombinant enzyme do not release acetate from acetylated xylan or mannan
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetylated rhamnogalacturonan I + H2O
acetate + deacetylated rhamnogalacturonan I
show the reaction diagram
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
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pH 6.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 6
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upon prolonged incubation the recombinant enzyme hydrolyses acetyl groups from modified hairy regions from apples to the same extent at pH 3.5 as at pH 6.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26350
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x * 26350, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 26350, calculated from sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure refined to a resolution of 1.12 A using synchrotron data collected at 263 K
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crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form is obtained at pH 5.0 and the trigonal crystal form at pH 4.5
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crystals used for structure determination are grown in 1.4 M Li2SO4, 0.1 M Na acetate pH 5.0 with a protein concentration of 40 OD280. The crystals belong to the space group P212121 with a = 52.14 A, b = 56.87 A and c = 71.89 A and one molecule in the asymmetric unit.The structure of RGAE is determined at 1.55 A resolution. RGAE folds into an alpha/beta/alpha structure. The active site of RGAE is an open cleft containing a serine-histidine-aspartic acid catalytic triad. The position of the three residues relative to the central parallel beta sheet and the lack of the nucleophilic elbow motif found in structures possessing the alpha/beta hydrolase fold shows that RGAE does not belong to the alpha/beta hydrolase family
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hanging-drop vapour-diffusion method
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vapour-diffusion method, the crystal structure of rhamnogalacturonan acetylesterase D192N is determined to 1.33 A resolution and refined to an R value of 11.6% for all data. The structure is virtually identical to the high-resolution (1.12 A) structure of the wild-type enzyme except for the interactions involving the mutation and a disordered loop
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Aspergillus oryzae
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of rhamnogalacturonan degrading enzymes by Aspergillus aculeatus is regulated at the level of transcription and is subjected to carbon catabolite repression by glucose
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