Glucanase | |||||||||
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Identifiers | |||||||||
EC no. | 3.2.1. | ||||||||
CAS no. | 9015-78-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Glucanase | |||||||
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Identifiers | |||||||
Symbol | Eng1p | ||||||
CAS number | |||||||
PDB | 5GY3 | ||||||
RefSeq | WP_012967086.1 | ||||||
UniProt | A0A0J4VP90 | ||||||
Other data | |||||||
EC number | 3.2.1 | ||||||
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Glucanases are enzymes that break down large polysaccharides via hydrolysis. The product of the hydrolysis reaction is called a glucan, a linear polysaccharide made of up to 1200 glucose monomers, held together with glycosidic bonds. [1] Glucans are abundant in the endosperm cell walls of cereals such as barley, rye, sorghum, rice, and wheat. [1] Glucanases are also referred to as lichenases, hydrolases, glycosidases, glycosyl hydrolases, and/or laminarinases. [1] Many types of glucanases share similar amino acid sequences but vastly different substrates. [1] Of the known endo-glucanases, 1,3-1,4-β-glucanase is considered the most active. [1]
The secondary and tertiary structures of β-glucanases involves the stacking of multiple β-sheets, each of which are made of several anti-parallel strands that bend and form a cleft crossing the active site of the enzyme. [1] This type of structure has been called the "jelly roll fold."
The functional formation of the enzyme-substrate complex is dictated by the induced-fit mechanism. [1]
The main function of glucanase is to catalyze the hydrolysis of glycosidic bonds in polysaccharides. This function is not highly specific, and the enzymes distinguish among substrates mostly by the types of bonds present and α- or β- configuration. [3]
In 1953, Dr. D. E. Koshland proposed a double-displacement mechanism for this enzyme action. [4] The first step of his proposed mechanism is rate-limiting step independent of the concentration of the substrate and involves an amino acid nucleophile and an acid/base catalyst. [4] In this step, the nucleophile, with help from the acid residue, displaces the aglycone and forms a covalent glycosyl-enzyme intermediate. [4] [1] The second step involves a water molecule, assisted by the conjugate base of the acid catalyst, rendering the free sugar while retaining an anomeric configuration of the molecule. [1]
Glucanases can also catalyze transglycosylation, resulting in new β-glycosidic bonds between donor and acceptor saccharides. [1] This reaction, which has the same region- and stereo-specificity as the hydrolysis reaction, involves either the direct reversal of hydrolysis (known as condensation) or kinetic control of a glycosyl donor substrate. [1]
Bacteria such as Escherichia coli , and Bacillus spp. produce 1,3-1,4-β-glucanases in order to degrade and use polysaccharides from their environment as an energy source. [1] These bacterial glucanases are an example of convergent evolution as they share similarity or relation with plant glucanase primary, secondary, or tertiary structure. [1] Glucanases have also been found to be secreted by fungi such as Trichoderma harzianum , Saccharomyces cerevisiae and the anaerobic fungi Orpinomyces and Neocallimastigomycota, found in the digestive tracts of herbivores. [1] [5] [6] T. harzianum is also used as a fungicide, which is linked to the ability of its β-gluanases to hydrolyze phytopathogenic fungi via a mycoparasitic attack. [6]
Barley 1,3-1,4-β-glucanases are heat inactivated during malting, which can cause the build-up of high molecular-weight glucans which in turn result in reduced extract yield, lower filtration rates, and even gelatinous precipitates in the finished product. As a remedy, heat-resistant bacterial 1,3-1,4-β-glucanases are added. [1]
Used in enological practices during the aging process of wine, particularly when aged on lees with microxygenation. The enzyme aids in autolysis of yeast cells to release polysaccharides and mannoproteins, which is believed to aid in the color and texture of the wine.
In the production of feedstuff for broiler chickens and piglets, it has been found that β-glucanases improve digestibility of barley-based diets. [1]
Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
A glucan is a polysaccharide derived from D-glucose, linked by glycosidic bonds. Glucans are noted in two forms: alpha glucans and beta glucans. Many beta-glucans are medically important. They represent a drug target for antifungal medications of the echinocandin class.
β-Amylase is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. It catalyses the following reaction:
β-Glucosidase is an enzyme that catalyses the following reaction:
The term glycosynthase refers to a class of proteins that have been engineered to catalyze the formation of a glycosidic bond. Glycosynthase are derived from glycosidase enzymes, which catalyze the hydrolysis of glycosidic bonds. They were traditionally formed from retaining glycosidase by mutating the active site nucleophilic amino acid to a small non-nucleophilic amino acid. More modern approaches use directed evolution to screen for amino acid substitutions that enhance glycosynthase activity.
In biochemistry, glycoside hydrolases are a class of enzymes which catalyze the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes, with roles in nature including degradation of biomass such as cellulose (cellulase), hemicellulose, and starch (amylase), in anti-bacterial defense strategies, in pathogenesis mechanisms and in normal cellular function. Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds.
Glucan 1,4-α-glucosidase is an enzyme located on the brush border of the small intestine with systematic name 4-α-D-glucan glucohydrolase. It catalyses the following chemical reaction
In enzymology, a xyloglucan-specific endo-beta-1,4-glucanase (EC 3.2.1.151) is an enzyme that catalyzes the chemical reaction
In enzymology, a xyloglucan-specific exo-beta-1,4-glucanase (EC 3.2.1.155) is an enzyme that catalyzes the chemical reaction
In molecular biology, Glycoside hydrolase family 12 is a family of glycoside hydrolases.
In molecular biology, Glycoside hydrolase family 16 is a family of glycoside hydrolases.
In molecular biology, glycoside hydrolase family 3 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of over 100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
In molecular biology, glycoside hydrolase family 92 is a family of glycoside hydrolases.
In molecular biology, glycoside hydrolase family 26 is a family of glycoside hydrolases.
Endo-1,3(4)-β-glucanase -β-D-glucan 3(4)-glucanohydrolase) is an enzyme with systematic name 3(or 4)-β-D-glucan 3(4)-glucanohydrolase. It catalyses the following chemical reaction
Glucan endo-1,3-α-glucosidase is an enzyme with systematic name 3-α-D-glucan 3-glucanohydrolase. It catalyses endohydrolysis of (1→3)-α-D-glucosidic linkages in isolichenan, pseudonigeran and nigeran
Lichenase is an enzyme with systematic name (1→3)-(1→4)-β-D-glucan 4-glucanohydrolase. It was named after its activity in on lichenin.
The enzyme glucan 1,4-β-glucosidase, also known as 4-β-D-glucan glucohydrolase, catalyses the hydrolysis of (1→4)-linkages in 1,4-β-D-glucans and related oligosaccharides, removing successive glucose units.
Glucan endo-1,6-β-glucosidase is an enzyme with systematic name 6-β-D-glucan glucanohydrolase. It catalyses random hydrolysis of (1→6)-linkages in (1→6)-β-D-glucans
Neopullulanase is an enzyme of the alpha-amylase family with systematic name pullulan 4-D-glucanohydrolase (panose-forming). This enzyme principally catalyses the following chemical reaction by cleaving pullulan's alpha-1,4-glucosidic bonds: