Amylase

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Human salivary amylase. Calcium ion visible in pale khaki; chloride ion in green. From PDB 1SMD.
amylase, alpha 1A; salivary
Identifiers
Symbol	AMY1A AMY1
HUGO	474
Entrez	276
OMIM	104700
RefSeq	NM_001008221
UniProt	P04745
PDB	1SMD
Other data
EC number	3.2.1.1
Locus	Chr. 1 p21

Human pancreatic amylase. Calcium ion visible in pale khaki; chloride ion in green. From PDB 1HNY.
amylase, alpha 2A; pancreatic
Identifiers
Symbol	AMY2A AMY2
HUGO	477
Entrez	279
OMIM	104650
RefSeq	NM_000699
UniProt	P04746
PDB	1HNY
Other data
EC number	3.2.1.1
Locus	Chr. 1 p21.1

Glucosidase, alpha, acid; lysosomal alpha-glucosidase
Identifiers
Symbol	GAA LYAG, MGAM
HUGO	[1]
Entrez	2548
OMIM	606800
RefSeq	NM_000152
UniProt	P10253
Other data
EC number	3.2.1.20
Locus	Chr. 17 q25.2-q25.3

Amylase is the name given to glycoside hydrolase enzymes that break down starch into glucose molecules. Although the amylases are designated by different Greek letters, they all act on α-1,4-glucosidic bonds.

Contents 1 Classification 1.1 α-Amylase 1.2 β-Amylase 1.3 γ-Amylase 1.4 Acid α-glucosidase 2 Amylase in human physiology 2.1 Salivary amylase (ptyalin) 2.1.1 Optimum conditions for ptyalin 2.2 Pancreatic amylase 3 Amylase in human pathology 3.1 Pompe disease 3.2 Pancreatitis 3.2.1 Detection 3.2.2 Interpretation 4 References 5 Uses 6 References 7 External links

[edit] Classification

[edit] α-Amylase

(EC 3.2.1.1 ) (CAS# 9014-71-5) (alternate names: 1,4-α-D-glucan glucanohydrolase; glycogenase) The α-amylases are calcium metalloenzymes, completely unable to function in the absence of calcium. By acting at random locations along the starch chain, α-amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. Because it can act anywhere on the substrate, α-amylase tends to be faster acting than β-amylase. In animals, it is a major digestive enzyme.

[edit] β-Amylase

(EC 3.2.1.2 ) (alternate names: 1,4-α-D-glucan maltohydrolase; glycogenase; saccharogen amylase) Another form of amylase, β-amylase is also synthesized by bacteria, fungi and plants. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. During the ripening of fruit, β-amylase breaks starch into sugar, resulting in the sweet flavor of ripe fruit. Both are present in seeds; β-amylase is present prior to germination whereas α-amylase and proteases appear once germination has begun. Cereal grain amylase is key to the production of malt. Many microbes also produce amylase to degrade extracellular starches. Animal tissues do not contain β-amylase, although it may be present in microrganisms contained within the digestive tract.

[edit] γ-Amylase

(EC 3.2.1.3 ) (alternative names: Glucan 1,4-α-glucosidase; amyloglucosidase; Exo-1,4-α-glucosidase; glucoamylase; lysosomal α-glucosidase; 1,4-α-D-glucan glucohydrolase) In addition to cleaving the last α(1-4)glycosidic linkages at the nonreducing end of amylose and amylopectin, yielding glucose, γ-amylase will cleave α(1-6) glycosidic linkages.

[edit] Acid α-glucosidase

Acid α-glucosidase (GAA) (EC 3.2.1.20 ) (alternative names: maltase-glucoamylase, MGAM; acid maltase; glucoinvertase; glucosidosucrase; lysosomal α-glucosidase; maltase) is found in the mammalian intestine has similar enzymatic activity to γ-amylase. Deficiencies of this enzyme result in Pompe Disease.

[edit] Amylase in human physiology

Although found in many tissues, amylase is most prominent in pancreatic juice and urine which each have their own isoform of human α-amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies. In humans, all amylase isoforms link to chromosome 1p21.

[edit] Salivary amylase (ptyalin)

Amylase is found in saliva and breaks starch down into maltose and dextrin. This form is also called ptyalin. Ptyalin will break large, insoluble starch molecules into soluble starches(amylodextrin,erythrodextrin,achrodextrin) producing successively smaller starches and ultimately maltose. Ptyalin acts on linear α(1,4) glucosidic linkages, but compound hydrolysis requires an enzyme which acts on branched products. Salivary amylase is inactivated in the stomach by gastric acid.

[edit] Optimum conditions for ptyalin

Optimum pH - 5.6–6.9

Human body temperature - 37 degrees Celsius

Presence of certain anions and activators:

Chlorine and bromine - most effective

Iodine - less effective

Sulfate and phosphate - least effective

[edit] Pancreatic amylase

Pancreatic α-amylase randomly cleaves the α(1-4)glycosidic linkages of amylose to yield dextrin, maltose or glucose molecules. It adopts a double displacement mechanism with retention of anomeric configuration.

[edit] Amylase in human pathology

[edit] Pompe disease

Deficiencies in γ-amylase function result in accumulation of intracellular material. The enzyme is also call acid lysosomal α-glucosidase or acid maltase to reflect the enzyme's intracellular function. The condition is known principally as glycogen storage disease, type II or Pompe Disease.

[edit] Pancreatitis

[edit] Detection

The test for amylase is easier to perform than lipase, making it the primary test used to test for and monitor pancreatitis. Labs will usually measure either pancreatic amylase, or total amylase. If only pancreatic amylase is measured, an increase will not be noted with mumps or other salivary gland trauma.

Unfortunately, because of the small amount present, timing is critical when sampling blood for this measurement. Blood should preferably be taken soon after a bout of pancreatitis pain, otherwise it is excreted rapidly by the kidneys.

[edit] Interpretation

Increased plasma levels in humans are found in:

• Salivary trauma (including anaesthetic intubation).
• Mumps — due to inflammation of the salivary glands.
• Pancreatitis — because of damage to the cells that produce amylase.
• Renal failure — due to reduced excretion.

Total amylase readings of over 10X the upper limit of normal (ULN) are suggestive of pancreatitis. 5-10x times the ULN may indicate ileus or duodenal disease or renal failure, and lower elevations are commonly found in salivary gland disease.

[edit] References

Burtis, Carl A.; Ashwood, Edward R. (1999). Tietz Textbook of Clinical Chemistry, 3rd ed.. Philadelphia: W. B. Saunders Company, 689-698, 1318. ISBN 0-7216-5610-2. 

[edit] Uses

Amylase enzymes are used extensively in bread making to break down complex sugars such as starch (found in flour) into simple sugars. Yeast then feeds on these simple sugars and converts it into the waste products of alcohol and CO2. This imparts flavour and causes the bread to rise. While Amylase enzymes are found naturally in yeast cells, it takes time for the yeast to produce enough of these enzymes to break down significant quantities of starch in the bread. This is the reason for long fermented doughs such as sour dough. Modern bread making techniques have included amyalse enzymes into bread improver thereby making the bread making process faster and more practical for commercial use.

Bacilliary amylase is also used in detergents to dissolve starches from fabrics.

Workers in factories that work with amylase for any of the above uses are at increased risk of asthma ("occupational asthma"). 5-9% of bakers have a positive skin test, and a fourth to a third to a third of bakers with breathing problems are hypersensitive to amylase.^[1]

[edit] References

1. ^ Mapp CE. Agents, old and new, causing occupational asthma. Occup Environ Med 2001;58:354-60. PMID 11303086.

[edit] External links

• Molecule of the month February 2006 at the Protein Data Bank.
• Nutrition Sciences 101 at University of Arizona.