Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
the enzyme belongs to the glucohydrolase family 12, GH12
evolution
-
the enzyme belongs to the glycoside hydrolase family 12, GH12
evolution
the enzyme belongs to the glycoside hydrolase family 74, GH74
evolution
the enzyme is a member of GH family 12, GH12
evolution
-
the enzyme belongs to the glycosyl hydrolase family 12, GH12
evolution
evolutionary relationship of persimmon DkXTH6 and DkXTH7 genes among other plant species and phylogenetic tree, overview. DkXTH6 and DkXTH7 possess several functional domains typical in plant XTHs, including the conserved amino acids (DEIDFEFLG) as a putative active site and together with a potential N-linked glycosylation (N-X-S/T) site
evolution
Paenibacillus odorifer produces a single multimodular enzyme containing a glycoside hydrolase (GH) family 74 module (AIQ73809). Endo-xyloglucanases, which catalyze the cleavage of the xyloglucans (XyGs) backbone (EC 3.2.1.151), are currently found in glycoside hydrolase (GH) families GH5, GH9, GH12, GH16, GH44, and GH74 (in CAZy classification). Of these, family GH74 is distinguished by fewer sequence members, an essentially singular specificity for xyloglucans, and a characteristic tertiary structure comprised of two 7-bladed beta-propeller domains that form a large interfacial cleft to accommodate the bulky polysaccharide
evolution
the enzyme belongs to the glycosyl hydrolase family 74, GH74. Myceliophthora thermophila strain VKPM F-244 produces two xyloglucan-degrading proteins with MWs of about 24 and 80 kDa. The 80 kDa protein is subjected to MALDI-TOF mass spectrometry peptide fingerprinting. Analysis of the data reveals maximal homology with the putative GH74 xyloglucanase from Myceliophthora thermophila ATCC 42464. The mtXgh74 gene encoding a GH74 xyloglucanase from strain VKPM F-244 is isolated using primers designed on the base of the MYCTH_116384 gene encoding AEO58927.1. The sequence of mtXgh74 is shown to be identical to MYCTH_116384
evolution
the enzyme belongs to the glycosyl hydrolase family 74, GH74. The CJA_2477 gene product comprises an N-terminal glycoside hydrolase family 74 (GH74) endo-xyloglucanase module in train with two carbohydrate-binding modules (CBMs) from families 10 and 2 (CBM10 and CBM2)
evolution
the XTH isozymes contain the conserved DEIDFEFLG motif identified as the catalytic domain of XTH
evolution
the endo-xyloglucanase belongs to the bacterial glycoside hydrolase family 74, GH74. Endo-xyloglucanases, which catalyze the cleavage of the XyGs backbone (EC 3.2.1.151), are currently found in glycoside hydrolase (GH) families GH5, GH9, GH12, GH16, GH44, and GH74 in the carbohydrate-active enzymes (CAZy) classification. Of these, family GH74 is distinguished by fewer sequence members, an essentially singular specificity for XyGs, and a characteristic tertiary structure comprised of two 7-bladed beta-propeller domains that form a large interfacial cleft to accommodate the bulky polysaccharide. Structure-activity relationships among characterized GH74 members, including determinants of endo versus exo (EC 3.2.1.150) activity, have been reviewed
evolution
the enzyme belongs to the endo-xyloglucanase family 74, GH74, family of enzymes. Phylogenetic diversity and catalytic mechanism of GH74 xyloglucanases from Ascomycete fungi, analysis of genome-wide distribution of GH74-encoding genes in ascomycetes, overview
evolution
-
the enzyme belongs to the glycosyl hydrolase family 74, GH74. Myceliophthora thermophila strain VKPM F-244 produces two xyloglucan-degrading proteins with MWs of about 24 and 80 kDa. The 80 kDa protein is subjected to MALDI-TOF mass spectrometry peptide fingerprinting. Analysis of the data reveals maximal homology with the putative GH74 xyloglucanase from Myceliophthora thermophila ATCC 42464. The mtXgh74 gene encoding a GH74 xyloglucanase from strain VKPM F-244 is isolated using primers designed on the base of the MYCTH_116384 gene encoding AEO58927.1. The sequence of mtXgh74 is shown to be identical to MYCTH_116384
-
evolution
-
the enzyme belongs to the glucohydrolase family 12, GH12
-
evolution
-
the enzyme belongs to the endo-xyloglucanase family 74, GH74, family of enzymes. Phylogenetic diversity and catalytic mechanism of GH74 xyloglucanases from Ascomycete fungi, analysis of genome-wide distribution of GH74-encoding genes in ascomycetes, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 74, GH74
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 74, GH74. Myceliophthora thermophila strain VKPM F-244 produces two xyloglucan-degrading proteins with MWs of about 24 and 80 kDa. The 80 kDa protein is subjected to MALDI-TOF mass spectrometry peptide fingerprinting. Analysis of the data reveals maximal homology with the putative GH74 xyloglucanase from Myceliophthora thermophila ATCC 42464. The mtXgh74 gene encoding a GH74 xyloglucanase from strain VKPM F-244 is isolated using primers designed on the base of the MYCTH_116384 gene encoding AEO58927.1. The sequence of mtXgh74 is shown to be identical to MYCTH_116384
-
evolution
-
the enzyme belongs to the endo-xyloglucanase family 74, GH74, family of enzymes. Phylogenetic diversity and catalytic mechanism of GH74 xyloglucanases from Ascomycete fungi, analysis of genome-wide distribution of GH74-encoding genes in ascomycetes, overview
-
evolution
-
the enzyme belongs to the endo-xyloglucanase family 74, GH74, family of enzymes. Phylogenetic diversity and catalytic mechanism of GH74 xyloglucanases from Ascomycete fungi, analysis of genome-wide distribution of GH74-encoding genes in ascomycetes, overview
-
evolution
-
the enzyme belongs to the endo-xyloglucanase family 74, GH74, family of enzymes. Phylogenetic diversity and catalytic mechanism of GH74 xyloglucanases from Ascomycete fungi, analysis of genome-wide distribution of GH74-encoding genes in ascomycetes, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 74, GH74
-
evolution
-
the endo-xyloglucanase belongs to the bacterial glycoside hydrolase family 74, GH74. Endo-xyloglucanases, which catalyze the cleavage of the XyGs backbone (EC 3.2.1.151), are currently found in glycoside hydrolase (GH) families GH5, GH9, GH12, GH16, GH44, and GH74 in the carbohydrate-active enzymes (CAZy) classification. Of these, family GH74 is distinguished by fewer sequence members, an essentially singular specificity for XyGs, and a characteristic tertiary structure comprised of two 7-bladed beta-propeller domains that form a large interfacial cleft to accommodate the bulky polysaccharide. Structure-activity relationships among characterized GH74 members, including determinants of endo versus exo (EC 3.2.1.150) activity, have been reviewed
-
evolution
-
Paenibacillus odorifer produces a single multimodular enzyme containing a glycoside hydrolase (GH) family 74 module (AIQ73809). Endo-xyloglucanases, which catalyze the cleavage of the xyloglucans (XyGs) backbone (EC 3.2.1.151), are currently found in glycoside hydrolase (GH) families GH5, GH9, GH12, GH16, GH44, and GH74 (in CAZy classification). Of these, family GH74 is distinguished by fewer sequence members, an essentially singular specificity for xyloglucans, and a characteristic tertiary structure comprised of two 7-bladed beta-propeller domains that form a large interfacial cleft to accommodate the bulky polysaccharide
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 74, GH74. The CJA_2477 gene product comprises an N-terminal glycoside hydrolase family 74 (GH74) endo-xyloglucanase module in train with two carbohydrate-binding modules (CBMs) from families 10 and 2 (CBM10 and CBM2)
-
malfunction
the enzyme hydrolytic activity is essentially completely eliminated in AtXTH31/AtXTH32 double knockout lines. Despite the elimination of enzyme hydrolase activity in initiating root hairs in the xth31/xth32 mutant, root hair initiation nonetheless appears to be grossly unaffected
malfunction
replacement of catalytic Gly476 with Tyr, which is conserved in many GH74 members, results in exclusive hydrolysis of xyloglucan at unbranched glucose units. Likewise, systematic replacement of the hydrophobic platform residues constituting the positive subsites indicated their relative contributions to the processive mode of action. Specifically, W347 (+3 subsite) and W348 (+5 subsite) are essential for processivity, while W406 (+2 subsite) and Y372 (+6 subsite) are not strictly essential, but aid processivity
malfunction
-
the enzyme hydrolytic activity is essentially completely eliminated in AtXTH31/AtXTH32 double knockout lines. Despite the elimination of enzyme hydrolase activity in initiating root hairs in the xth31/xth32 mutant, root hair initiation nonetheless appears to be grossly unaffected
-
malfunction
-
replacement of catalytic Gly476 with Tyr, which is conserved in many GH74 members, results in exclusive hydrolysis of xyloglucan at unbranched glucose units. Likewise, systematic replacement of the hydrophobic platform residues constituting the positive subsites indicated their relative contributions to the processive mode of action. Specifically, W347 (+3 subsite) and W348 (+5 subsite) are essential for processivity, while W406 (+2 subsite) and Y372 (+6 subsite) are not strictly essential, but aid processivity
-
metabolism
the enzyme from the saprophytic Gram-negative bacterium catalyzes the first step of xyloglucan degradation. The GH74 catalytic domain generates Glc4-based xyloglucooligosaccharide (XyGO) substrates for downstream enzymes through an endo-dissociative mode of action
metabolism
-
the enzyme from the saprophytic Gram-negative bacterium catalyzes the first step of xyloglucan degradation. The GH74 catalytic domain generates Glc4-based xyloglucooligosaccharide (XyGO) substrates for downstream enzymes through an endo-dissociative mode of action
-
physiological function
-
XEG has a dose-dependent effect on seedling growth, morphology, cell wall, and xyloglucan composition
physiological function
isoform XTH2 is associated with petal growth and development during carnation flower opening
physiological function
isoform XTH3 is associated with petal growth and development during carnation flower opening
physiological function
-
XTH3 transgenic tomato plants exhibit a markedly increased tolerance to salt and drought stresses. Transgenic tomato plants exposed to a salt stress of 100 mM NaCl retain the chlorophyll in their leaves and shows normal root elongation. They also remain green and unwithered following exposure to 2 weeks of dehydration. Despite this increased stress tolerance, the transgenic tomato plants show no detectable phenotype defects
physiological function
xyloglucan endohydrolysis is a latent activity in the root cell wall remaining from the period of cell elongation (where, in particular, AtXTH31 transcript levels are high), which is not strictly essential for root hair initiation
physiological function
xyloglucan is a major component of the cell wall in most plants, and xyloglucan-specific endo-beta-1,4-glucanase digests the polysaccharide chains of plant cell walls. To protect the cell wall from these enzymes, plants secrete glycoside hydrolase inhibitor proteins
physiological function
a molecule of tamarind xyloglucan has a certain structural regularity: it is composed of 1,4-beta-D-glucotetraose units, where three glucosyl residues modified with a D-xylose via alpha-1,6-glycosidic bonds are followed by an unbranched glucosyl residue. The D-xyloses may be decorated with beta-1,2-D-galactosyl or to small amounts with alpha-1,2-L-arabinosyl residues. Degradation of xyloglucan requires a broad range of hydrolases with different activities and specificities, including extracellular Xgh74 endoxyloglucanase
physiological function
a role for enzyme XTH31 in acid growth. Isozymes XTH15 and XTH31 are both strongly expressed in young, rapidly growing organs, suggesting that they play roles in cell expansion. In vitro, XTH15 has very high transglucanase (endotransglucosylase, XET) but undetectable hydrolytic activity (glucanase, XEH). In contrast, XTH31 has very high XEH activity and only slight XET activity
physiological function
isozymes XTH15 and XTH31 are both strongly expressed in young, rapidly growing organs, suggesting that they play roles in cell expansion. In vitro, XTH15 has very high transglucanase (endotransglucosylase, XET) but undetectable hydrolytic activity (glucanase, XEH). In contrast, XTH31 has very high XEH activity and only slight XET activity
physiological function
several XTH isozymes function in persimmon (Diospyros kaki) fruit development and postharvest softening. Isozymes DkXTH1, DkXTH4, and DkXTH5 expressions peak in immature expanding fruit, and their higher expression is observed along with higher fruit firmness in cold-treated fruit or firmer cultivar fruit during storage. The opposite gene expression patterns are observed in DkXTH2 and DkXTH3, which reach maxima concomitance with pronounced fruit softening. Meanwhile, the xyloglucan endotransglycosylase (XET, EC 2.4.1.207) enzymes play important roles in both the rapid growth and ripening of persimmon fruit. Furthermore, the recombined DkXTH1 and DkXTH2 proteins show significant XET activity without any detected XEH (EC 3.2.1.151) activity
physiological function
-
the fungal symbiont provides a single xyloglucanase (Xeg1) to its ant farmers by upregulating the expression of this protein in the inflated hyphal tips (gongylidia) that the ants ingest. Similar to other enzymes ingested this way, also Xeg1 is not digested but vectored to the fresh leaf-fragment pulp at the top of fungus gardens via ant fecal fluid. Xeg1 is 4-5 times more active in fecal fluid when ants ingest their normal fungal food, compared to a sucrose control diet, as expected when they cannot produce Xeg1 themselves. Ingestion of the enzyme by the ants for transfer to the fecal fluid is actively promoted by the fungal symbiont
physiological function
the holoparasitic angiosperm Cuscuta develops haustoria that enable it to feed on other plants, e.g. tomato plants. Cell wall modifications seem to be required in order for the parasite to successfully infect a host, changes to xyloglucan through the activity of xyloglucan endotransglucosylases/hydrolases (XTHs) are essential. On the other hand, XTH expression is also detected in resistant tomato upon an attack by Cuscuta, which suggests that both host and parasite use these enzymes in their arms race. Cell wall-modifying activities of XTHs during parasitization , overview. XTHs might function to make the host's resources accessible to Cuscuta. One of the defense responses of Solanum lycopersicum is the increased expression of LeXTH1, a gene encoding an XTH. The function of LeXTH1 might be to promote the elongation of tomato epidermal cells that takes place at the site of contact with the parasite. Another possibility is that LeXTH1 is deployed to reinforce the tomato cell walls, presumably as a remedy against the cell wall loosening activity of Cuscuta XTHs at the interface. Increased levels of xyloglucan degradation occur in the haustorium of Cuscuta reflexa and in the infected Solanum lycopersicum host plant
physiological function
-
the holoparasitic angiosperm Cuscuta develops haustoria that enable it to feed on other plants, e.g. tomato plants. Cell wall modifications seem to be required in order for the parasite to successfully infect a host, changes to xyloglucan through the activity of xyloglucan endotransglucosylases/hydrolases (XTHs) are essential. On the other hand, XTH expression is also detected in resistant tomato upon an attack by Cuscuta, which suggests that both host and parasite use these enzymes in their arms race. Cell wall-modifying activities of XTHs during parasitization, overview. XTHs might function to make the host's resources accessible to Cuscuta. At the onset of haustorium development, the swelling of the parasite stem facing the host plant is facilitated by Cuscuta XTHs that promote expansive cell growth through wall loosening. As the haustorium begins its host-invasive growth, XTHs secreted from the infection organ aid tissue penetration by loosening host cell walls. Upon reaching the vascular bundles of its host, the cell wall loosening activity of Cuscuta XTHs at the host-parasite interface enables parasite feeding through apoplastic sugar transfer and/or by promoting vascular tissue differentiation. To prevent exaggerated cell wall loosening under low turgor pressure, Cuscuta XTHs must also strengthen its own walls. When Cuscuta attempts to invade cultivated tomato by deploying wall loosening XTHs at the interface, the counteractive wall strengthening activity of host-encoded XTHs prevents the haustorium from entering the host plant. Model of the putative function of XTHs in the parasitization strategy of Cuscuta, increased levels of xyloglucan degradation occur in the haustorium of Cuscuta reflexa and in the infected Solanum lycopersicum host plant
physiological function
XTH, an important enzyme involved in xyloglucan metabolism, can function as a xyloglucan endotransglycosylase (XET, EC 2.4.1.207) and/or a xyloglucan endohydrolase (XEH, EC 3.2.1.151), with the former transferring one xyloglucan molecule fragment to another and the latter responsible for hydrolysis of one xyloglucan molecule. DkXTH7 is likely to be involved in cell wall assembly, special roles of isozyme XTH6 and XTH7 in persimmon fruit softening, overvie. The XTH gene family members each play a certain role in plant growth, fruit ripening, and fruit softening. During persimmon fruit postharvest softening,expression of isozymes DkXTH6 and DkXTH7 follows two opposing patterns
physiological function
XTH, an important enzyme involved in xyloglucan metabolism, can function as a xyloglucan endotransglycosylase (XET, EC 2.4.1.207) and/or a xyloglucan endohydrolase (XEH, EC 3.2.1.151), with the former transferring one xyloglucan molecule fragment to another and the latter responsible for hydrolysis of one xyloglucan molecule. Enzyme DkXTH6 might take part in cell wall restructuring, special roles of isozyme XTH6 and XTH7 in persimmon fruit softening, overview. The XTH gene family members each play a certain role in plant growth, fruit ripening, and fruit softening. During persimmon fruit postharvest softening,expression of isozymes DkXTH6 and DkXTH7 follows two opposing patterns
physiological function
endo-xyloglucanases from the GH74 family hydrolyze xyloglucans (XyGs). Enzymatic XyG hydrolysis increases cellulose digestibility, which underscores their structural importance in the plant cell wall. XyGs are also found as storage polysaccharides in some seeds, e.g. tamarind, and therefore represent important agricultural byproducts that have applications in the food, biomaterial and medical sectors. The endo-xyloglucanase can hydrolyze the regular structure of XXXG-type XyGs at the anomeric center of the unbranched glucosyl (G) unit, although some cleave the backbone at more sterically encumbered positions, e.g. between two X units
physiological function
enzyme AfXEG74 has no CBM modul and shows high specificity in xyloglucan hydrolysis. AfXEG74 does not cleave short xyloglucan oligosaccharides
physiological function
-
a molecule of tamarind xyloglucan has a certain structural regularity: it is composed of 1,4-beta-D-glucotetraose units, where three glucosyl residues modified with a D-xylose via alpha-1,6-glycosidic bonds are followed by an unbranched glucosyl residue. The D-xyloses may be decorated with beta-1,2-D-galactosyl or to small amounts with alpha-1,2-L-arabinosyl residues. Degradation of xyloglucan requires a broad range of hydrolases with different activities and specificities, including extracellular Xgh74 endoxyloglucanase
-
physiological function
-
enzyme AfXEG74 has no CBM modul and shows high specificity in xyloglucan hydrolysis. AfXEG74 does not cleave short xyloglucan oligosaccharides
-
physiological function
-
xyloglucan endohydrolysis is a latent activity in the root cell wall remaining from the period of cell elongation (where, in particular, AtXTH31 transcript levels are high), which is not strictly essential for root hair initiation
-
physiological function
-
a molecule of tamarind xyloglucan has a certain structural regularity: it is composed of 1,4-beta-D-glucotetraose units, where three glucosyl residues modified with a D-xylose via alpha-1,6-glycosidic bonds are followed by an unbranched glucosyl residue. The D-xyloses may be decorated with beta-1,2-D-galactosyl or to small amounts with alpha-1,2-L-arabinosyl residues. Degradation of xyloglucan requires a broad range of hydrolases with different activities and specificities, including extracellular Xgh74 endoxyloglucanase
-
physiological function
-
isoform XTH3 is associated with petal growth and development during carnation flower opening
-
physiological function
-
isoform XTH2 is associated with petal growth and development during carnation flower opening
-
physiological function
-
enzyme AfXEG74 has no CBM modul and shows high specificity in xyloglucan hydrolysis. AfXEG74 does not cleave short xyloglucan oligosaccharides
-
physiological function
-
enzyme AfXEG74 has no CBM modul and shows high specificity in xyloglucan hydrolysis. AfXEG74 does not cleave short xyloglucan oligosaccharides
-
physiological function
-
enzyme AfXEG74 has no CBM modul and shows high specificity in xyloglucan hydrolysis. AfXEG74 does not cleave short xyloglucan oligosaccharides
-
physiological function
-
endo-xyloglucanases from the GH74 family hydrolyze xyloglucans (XyGs). Enzymatic XyG hydrolysis increases cellulose digestibility, which underscores their structural importance in the plant cell wall. XyGs are also found as storage polysaccharides in some seeds, e.g. tamarind, and therefore represent important agricultural byproducts that have applications in the food, biomaterial and medical sectors. The endo-xyloglucanase can hydrolyze the regular structure of XXXG-type XyGs at the anomeric center of the unbranched glucosyl (G) unit, although some cleave the backbone at more sterically encumbered positions, e.g. between two X units
-
additional information
key amino acid residues for the endo-processive activity of GH74 xyloglucanase, an endo-processive xyloglucanase, are W318 and W319, found in the positive subsites. They are essential for processive degradation and are responsible for maintaining binding interactions with xyloglucan polysaccharide through a stacking effect, three-dimensional homology modelling, overview. The enzyme has four characteristic tryptophan residues (W61, W64, W318, and W319) around the active site cleft. Although W61 and W64 are dispensable for endo-processive xyloglucanase activity, these residues contribute slightly to endo-processive activity and/or substrate recognition
additional information
-
structure homology modelling using Aspergillus niger endoglucanase structure, PDB ID 1KS5
additional information
three-dimensional structure modelling, overview
additional information
the substrate binding site of CjGH74 lies in an open cleft at the intersection of the N- and C-terminal domains. The catalytic residues, Asp70 (catalytic base) and Asp483 (catalytic acid), are located on opposite sides in the middle of this cleft. Three-dimensional structure of enzyme CjGH74 in complex with xyloglucooligosaccharides, overview
additional information
-
the substrate binding site of CjGH74 lies in an open cleft at the intersection of the N- and C-terminal domains. The catalytic residues, Asp70 (catalytic base) and Asp483 (catalytic acid), are located on opposite sides in the middle of this cleft. Three-dimensional structure of enzyme CjGH74 in complex with xyloglucooligosaccharides, overview
additional information
mode of action of enzyme AfXEG74, overview. AfXEG74 hydrolyzes xyloglucan from tamarind (XyGt) by acting mainly on unbranched glucosyl residues (G), either before or after this position. In some cases, XX positions can also be attacked at specific points, for example when this motif is linked to the XG position that occurs in regions deprived of galactosyl branches
additional information
-
mode of action of enzyme AfXEG74, overview. AfXEG74 hydrolyzes xyloglucan from tamarind (XyGt) by acting mainly on unbranched glucosyl residues (G), either before or after this position. In some cases, XX positions can also be attacked at specific points, for example when this motif is linked to the XG position that occurs in regions deprived of galactosyl branches
additional information
-
structure homology modelling using Aspergillus niger endoglucanase structure, PDB ID 1KS5
-
additional information
-
three-dimensional structure modelling, overview
-
additional information
-
mode of action of enzyme AfXEG74, overview. AfXEG74 hydrolyzes xyloglucan from tamarind (XyGt) by acting mainly on unbranched glucosyl residues (G), either before or after this position. In some cases, XX positions can also be attacked at specific points, for example when this motif is linked to the XG position that occurs in regions deprived of galactosyl branches
-
additional information
-
mode of action of enzyme AfXEG74, overview. AfXEG74 hydrolyzes xyloglucan from tamarind (XyGt) by acting mainly on unbranched glucosyl residues (G), either before or after this position. In some cases, XX positions can also be attacked at specific points, for example when this motif is linked to the XG position that occurs in regions deprived of galactosyl branches
-
additional information
-
mode of action of enzyme AfXEG74, overview. AfXEG74 hydrolyzes xyloglucan from tamarind (XyGt) by acting mainly on unbranched glucosyl residues (G), either before or after this position. In some cases, XX positions can also be attacked at specific points, for example when this motif is linked to the XG position that occurs in regions deprived of galactosyl branches
-
additional information
-
mode of action of enzyme AfXEG74, overview. AfXEG74 hydrolyzes xyloglucan from tamarind (XyGt) by acting mainly on unbranched glucosyl residues (G), either before or after this position. In some cases, XX positions can also be attacked at specific points, for example when this motif is linked to the XG position that occurs in regions deprived of galactosyl branches
-
additional information
-
key amino acid residues for the endo-processive activity of GH74 xyloglucanase, an endo-processive xyloglucanase, are W318 and W319, found in the positive subsites. They are essential for processive degradation and are responsible for maintaining binding interactions with xyloglucan polysaccharide through a stacking effect, three-dimensional homology modelling, overview. The enzyme has four characteristic tryptophan residues (W61, W64, W318, and W319) around the active site cleft. Although W61 and W64 are dispensable for endo-processive xyloglucanase activity, these residues contribute slightly to endo-processive activity and/or substrate recognition
-
additional information
-
the substrate binding site of CjGH74 lies in an open cleft at the intersection of the N- and C-terminal domains. The catalytic residues, Asp70 (catalytic base) and Asp483 (catalytic acid), are located on opposite sides in the middle of this cleft. Three-dimensional structure of enzyme CjGH74 in complex with xyloglucooligosaccharides, overview
-