Literature summary for 3.2.1.179 extracted from

Germane, K.L.; Servinsky, M.D.; Gerlach, E.S.; Sund, C.J.; Hurley, M.M.
Structural analysis of Clostridium acetobutylicum ATCC 824 glycoside hydrolase from CAZy family GH105 (2015), Acta Crystallogr. Sect. F, 71, 1100-1108 .

Search for more literature for 3.2.1.179

Cloned(Commentary)

Cloned (Comment)	Organism
gene CA_C0359, recombinant expression of the intein-fused enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli TOP10, transcriptional analysis using quantitative PCR	Clostridium acetobutylicum

Crystallization (Commentary)

Crystallization (Comment)	Organism
partially purified recombinnat enzyme, hanging-drop vapor-diffusion method, mixing 0.002 ml 7.5 mg/ml protein solution with 0.002 ml reservoir solution consisting of 0.1 M Tris, pH 7.75, 16% w/v PEG 4000, 21°C, X-ray diffraction structure determination and analysis at 1.6 A resolution, modelling	Clostridium acetobutylicum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp + H2O	Clostridium acetobutylicum	-	5-dehydro-4-deoxy-D-glucuronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp	-	?

Organism

Organism	UniProt	Comment	Textmining
Clostridium acetobutylicum	Q97M41	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by ultrafiltration and gel filtration	Clostridium acetobutylicum

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	the enzyme expression is induced threefold and sixfold during growth on pectin and polygalacturonic acid, respectively, when compared with growth on glucose	Clostridium acetobutylicum	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp + H2O	-	Clostridium acetobutylicum	5-dehydro-4-deoxy-D-glucuronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp	-	?
additional information	the degradation of the polygalacturonan (PGA) and rhamnogalacturonan-I (RG-I) backbones of pectin. In both instances the unsaturated GalA may spontaneously open to 4-deoxy-L-threo-5-hexosulose-uronate, reaction pathways, overview. The suggested mechanism for both families, the unsaturated rhamnogalacturonyl hydrolase (EC 3.2.1.172) and the unsaturated glucuronyl hydrolase (EC 3.2.1.179), requires hydration at the C=C bond of the unsaturated sugar, resulting in glycosidic cleavage. Substrate specificity in the GH105 family correlates with the loops surrounding the active site	Clostridium acetobutylicum	?	-	?

Subunits

Subunits	Comment	Organism
More	the protein adopts a six-(alpha/alpha)-hairpin barrel fold with a small two-stranded beta-sheet and helix overlaying the end of the barrel near the active pocket. The CA_C0359 structure closely adopts the fold of family GH105 proteins	Clostridium acetobutylicum

Synonyms

Synonyms	Comment	Organism
CaUGL	-	Clostridium acetobutylicum
CA_C0359	-	Clostridium acetobutylicum
More	cf. EC 3.2.1.172	Clostridium acetobutylicum
UGL	-	Clostridium acetobutylicum
unsaturated glucuronyl hydrolase	-	Clostridium acetobutylicum

Expression

Organism	Comment	Expression
Clostridium acetobutylicum	the enzyme expression is induced threefold and sixfold during growth on pectin and polygalacturonic acid, respectively, when compared with growth on glucose	up

General Information

General Information	Comment	Organism
evolution	Clostridium acetobutylicum ATCC 824 gene CA_C0359 encodes a putative unsaturated rhamnogalacturonyl hydrolase (URH) with distant amino-acid sequence homology to YteR of Bacillus subtilis strain 168. YteR, like other URHs, has core structural homology to unsaturated glucuronyl hydrolases, but hydrolyzes the unsaturated disaccharide derivative of rhamnogalacturonan I. There is a conserved aspartic acid residue in both structures, which has been shown to be important for hydration of the C=C bond during the release of unsaturated galacturonic acid by YteR. A surface electrostatic potential comparison of CA_C0359 and proteins from CAZy families GH88 and GH105 reveals the make-up of the active site to be a combination of the unsaturated rhamnogalacturonyl hydrolase (EC 3.2.1.172) and the unsaturated glucuronyl hydrolase (EC 3.2.1.179) from Bacillus subtilis strain 168. Structural and electrostatic comparisons suggest that the enzyme may have a slightly different substrate specificity from that of YteR	Clostridium acetobutylicum
additional information	substrate-bound enzyme structure modeling, overview	Clostridium acetobutylicum

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Release 2023.1 (January 2023)