maltase
Information about maltase
Maltase (EC 3.2.1.20) is an enzyme produced by the cells lining the small intestine which specifically breaks down the disaccharide maltose. It comes under the enzyme category carbohydrase (which is a subcategory of hydrolase), and the disaccharide it hydrolyses is maltose.
Maltase is secreted by the surface cells of the villi, which are thin projections on the mucosa. These are found throughout the small intestine, but differ in shape in the duodenum and ileum sections.
The maltase works like any other enzyme, with the substrate (maltose) binding with the active site. When the maltose had bound with the maltase, the former is hydrolysed, that is to say it is split into its component parts, i.e. two molecules of α-glucose. This is done by breaking the glycosidic bond between the 'first' carbon of one glucose, and the 'fourth' carbon of the other (a 1-4 bond).
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Maltase is secreted by the surface cells of the villi, which are thin projections on the mucosa. These are found throughout the small intestine, but differ in shape in the duodenum and ileum sections.
The maltase works like any other enzyme, with the substrate (maltose) binding with the active site. When the maltose had bound with the maltase, the former is hydrolysed, that is to say it is split into its component parts, i.e. two molecules of α-glucose. This is done by breaking the glycosidic bond between the 'first' carbon of one glucose, and the 'fourth' carbon of the other (a 1-4 bond).
External links
References
- Solomon, Eldra P.; Berg, Linda R.; & Martin, Diana W. (2002). Biology (6th ed). Thomson Learning, Inc. ISBN 0-03-033503-5
External links
Hydrolase: sugar hydrolases (EC 3.2) | |
|---|---|
| 3.2.1: Glycoside hydrolases | Amylase (Alpha-Amylase) - Chitinase - Lysozyme - Neuraminidase - Galactosidases (Alpha, Beta) - alpha-Mannosidase - Glucuronidase - Hyaluronidase - Pullulanase - Glucocerebrosidase - Galactosylceramidase - Alpha-N-acetylglucosaminidase - Fucosidase - Hexosaminidase - Iduronidase - Disaccharidase (Sucrase/Sucrase-isomaltase/Invertase, Maltase, Trehalase, Lactase) - Glucosidases (Cellulase, Alpha-glucosidase, Beta-glucosidase, Debranching enzyme) |
| 3.2.2: Hydrolysing N-Glycosyl compounds | DNA glycosylases: Oxoguanine glycosylase |
Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
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Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions.[1] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products.
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In biology the small intestine is the part of the gastrointestinal tract (gut) between the stomach and the large intestine and includes the duodenum, jejunum, and ileum. It is where the vast majority of digestion takes place.
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A disaccharide is a sugar (a carbohydrate) composed of two monosaccharides.[1]
'Disaccharide' is one of the four chemical groupings of carbohydrates (monosaccharide, disaccharide, oligosaccharide, and polysaccharide).
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'Disaccharide' is one of the four chemical groupings of carbohydrates (monosaccharide, disaccharide, oligosaccharide, and polysaccharide).
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In biochemistry, a hydrolase is an enzyme that catalyzes the hydrolysis of a chemical bond. For example, an enzyme that catalyzed the following reaction is a hydrolase:
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- A–B + H2O → A–OH + B–H
Nomenclature
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Maltose, or malt sugar, is a disaccharide formed from two units of glucose joined with an α(1→4) linkage. It is the second member of an important biochemical series of glucose chains.
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Villus (Latin: "shaggy hair"[1], plural villi) can refer to:
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- Intestinal villus. This is the most common meaning when not more precisely specified
- Chorionic villi, found on the surface of the outermost membrane (the chorion) of the fetus
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The mucous membranes (or mucosae; singular: mucosa) are linings of mostly endodermal origin, covered in epithelium, and are involved in absorption and secretion. They line various body cavities that are exposed to the external environment and internal organs.
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In anatomy of the digestive system, the duodenum is a hollow jointed tube about 25-30 cm long connecting the stomach to the jejunum. It is the first and shortest part of the small intestine and it is where most chemical digestion takes place.
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ileum is the final section of the small intestine. It is about 2-4 m long in humans, follows the duodenum and jejunum, and is separated from the cecum by the ileocecal valve (ICV). The pH in the ileum is usually between 7 and 8 (neutral or slightly alkaline).
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In biochemistry, a substrate is a molecule upon which an enzyme acts. Enzymes catalyze chemical reactions involving the substrate(s). The substrate binds with the enzyme's active site, and an enzyme-substrate complex is formed.
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The active site of an enzyme contains the catalytic and binding sites. The structure and chemical properties of the active site allow the recognition and binding of the substrate.
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In chemistry, a glycosidic bond is a certain type of functional group that joins a carbohydrate (sugar) molecule to an alcohol, which may be another carbohydrate. Specifically, a glycosidic bond is formed between the hemiacetal group of a saccharide (or a molecule derived from a
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Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. Created and updated by the United States National Library of Medicine (NLM), it is used by the MEDLINE/PubMed
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In biochemistry, a hydrolase is an enzyme that catalyzes the hydrolysis of a chemical bond. For example, an enzyme that catalyzed the following reaction is a hydrolase:
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- A–B + H2O → A–OH + B–H
Nomenclature
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Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
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Glycoside hydrolases (also called glycosidases) catalyze the hydrolysis of the glycosidic linkage to generate two smaller sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial
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Amylase is the name given to glycoside hydrolase enzymes that break down starch into glucose molecules. Amylase is also known as Ptyalin. Although the amylases are designated by different Greek letters, they all act on α-1,4-glycosidic bonds.
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α-Amylase is the major form of amylase found in humans and other mammals.
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Amylase in human physiology
Although found in many tissues, amylase is most prominent in pancreatic juice and saliva which each have their own isoform of human α-amylase...... Click the link for more information.
Identifiers
Symbol CHIT1
Entrez 1118
HUGO 1936
OMIM 600031
RefSeq NM_003465
UniProt Q13231
Other data
Locus Chr. 1 q31-q32 Chitinase (barley seed chitinase: PDB 1CNS , EC 3.2.1.
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Symbol CHIT1
Entrez 1118
HUGO 1936
OMIM 600031
RefSeq NM_003465
UniProt Q13231
Other data
Locus Chr. 1 q31-q32 Chitinase (barley seed chitinase: PDB 1CNS , EC 3.2.1.
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Lysozyme is a 14.4 kilodalton enzyme (EC 3.2.1.17 ) that damages bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
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Neuraminidase is a glycoside hydrolase enzyme (EC 3.2.1.18 ). It is frequently found as an antigenic glycoprotein and is best known as one of the enzymes found on the surface of the Influenza virus.
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Galactosidases are enzymes (glycoside hydrolases) which catalyzes the hydrolysis of galactosides into monosaccharides
If the galactoside is an alpha-galactoside, the enzyme is called alpha-galactosidase, and if it is a beta-galactoside, it is called beta-galactosidase.
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If the galactoside is an alpha-galactoside, the enzyme is called alpha-galactosidase, and if it is a beta-galactoside, it is called beta-galactosidase.
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Alpha-galactosidase is a glycoside hydrolase generated from a gene on the X chromosome.
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Pathology
A deficiency is associated with Fabry's disease.See also
- Beano (dietary supplement)
- Beta-galactosidase
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- MeSH
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β-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins.
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Identifiers
Symbol MAN2C1
Alt. Symbols MANA1, MANA
Entrez 4123
HUGO 6827
OMIM 154580
RefSeq NM_006715
UniProt Q9NTJ4
Other data
EC number 3.2.1.24
Locus Chr.
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Symbol MAN2C1
Alt. Symbols MANA1, MANA
Entrez 4123
HUGO 6827
OMIM 154580
RefSeq NM_006715
UniProt Q9NTJ4
Other data
EC number 3.2.1.24
Locus Chr.
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Glucuronidases are glycoside hydrolases that cleave glucuronic acid glycosides (glucuronides). Human glucuronidase is a lysosomal glycosidase, and hydrolyzes glucuronide moieties from proteins.
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The hyaluronidases (EC 3.2.1.35 ) are a family of enzymes that degrade hyaluronic acid.
By catalyzing the hydrolysis of hyaluronic acid, a major constituent of the interstitial barrier, hyaluronidase lowers the viscosity of hyaluronic acid, thereby increasing tissue
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By catalyzing the hydrolysis of hyaluronic acid, a major constituent of the interstitial barrier, hyaluronidase lowers the viscosity of hyaluronic acid, thereby increasing tissue
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Pullulanase is a specific kind of glucanase, an amylolytic exoenzyme, that degrades pullulan. It is produced as an extracellular, cell surface-anchored lipoprotein by Gram-negative bacteria of the genus Klebsiella.
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Glucocerebrosidase (also called glucosylceramidase, β-glucosidase, or D-glucosyl-N-acylsphingosine glucohydrolase) is an enzyme (EC 3.2.1.45 ) that is needed to break down the chemical glucocerebroside by hydrolysis.
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