Other names in common use include glycerol dehydrase, and glycerol hydro-lyase.

The enzymes threonine deaminase, dihydroxy acid dehydrase and transaminase are controlled by end-product regulation.

This forms 13-hydroperoxylinolenic acid, which is then modified by a dehydrase and undergoes cyclization by allene oxide cyclase to form 12-oxo-phytodienoic acid.

The third reaction is the dehydration reaction of α, β-dihydroxyisovalerate catalyzed by Dihydroxy acid dehydrase resulting in α-ketoisovalerate.

Reuterin is a potent antimicrobial multi-compound produced by Lactobacillus reuteri, during the metabolism of glycerol to 1,3-propanediol catalysed by the coenzyme B12-dependent diol dehydrase.

The genes that encode both the Dihydroxy acid dehydrase used in the creation of α-ketoisovalerate and Transaminase E, as well as other enzymes are encoded on the ilvEDA operon.

A xylonate dehydratase is splitting off a water molecule resulting in 2-keto 3-deoxy-xylonate.

In addition, homocystinuria is a hereditary disease caused by the deficiency of L-serine dehydratase.

A second dehydratase forms the 2-keto glutarate semialdehyde which is subsequently oxidised to 2-ketoglutarate.

Other names in common use include inosose 2,3-dehydratase, ketoinositol dehydratase, and 2,4,6/3,5-pentahydroxycyclohexanone hydro-lyase.

ALA dehydratase deficiency is a rare cause of hepatic porphyria.

Imidazoleglycerol-phosphate dehydratase is an enzyme catalysing the sixth step of histidine production.

Most archaea lack ilvA, and only a limited number possess catabolic threonine dehydratase.

Serine dehydratase has also been found to be absent in human colon carcinoma and rat sarcoma.

Serine is then converted to pyruvate by serine dehydratase.

Serine Dehydratase is also known as:

ALA dehydratase deficiency is inherited in an autosomal recessive manner.

For example, serine dehydratase converts serine to pyruvate and ammonia.

L-Serine dehydratase condenses homocysteine with serine to form cystathionine.

Biosynthesis: The enzyme 3-dehydroquinate dehydratase uses 3-dehydroquinate to produce 3-dehydroshikimate and HO.

Two isomers are important, the 2- and 3-isopropyl derivatives, and these are interconverted by isopropylmalate dehydratase.

Dehydratase is an enzyme that catalyzes the removal of oxygen and hydrogen from organic compounds in the form of water.

It begins by the degradation of glycerol, a compound naturally found in wine at levels of 5-8 g/L, via a dehydratase enzyme to 3-hydroxypropionaldehyde.

In addition, researchers have shown that L-threonine competitively inhibits Serine Dehydratase as well.

Pterin-4-alpha-carbinolamine dehydratase is an enzyme that in humans is encoded by the PCBD1 gene.

As mentioned previously, two classes of 3-Dehydroquinate Dehydratase exist, known as types I and II.

Moreover, insulin is known to accelerate glycolysis and repress induction of liver serine dehydratase in adult diabetic rats.

In both Pseudomonas and Bordetella species P9 appears to be located upstream of a predicted threonine dehydratase gene.

In E. coli the enzyme encoded by the gene hisB is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase.

In overall terms, the reaction catalyzed by serine dehydratase involves two steps: catalytic elimination and a nonenzymatic hydrolysis reaction.

Studies have been conducted to show insulin causes a 40-50% inhibition of the induction serine dehydratase by glucagon in hepatocytes of rats.

A xylonate dehydratase is splitting off a water molecule resulting in 2-keto 3-deoxy-xylonate.

In addition, homocystinuria is a hereditary disease caused by the deficiency of L-serine dehydratase.

A second dehydratase forms the 2-keto glutarate semialdehyde which is subsequently oxidised to 2-ketoglutarate.

Other names in common use include inosose 2,3-dehydratase, ketoinositol dehydratase, and 2,4,6/3,5-pentahydroxycyclohexanone hydro-lyase.

ALA dehydratase deficiency is a rare cause of hepatic porphyria.

Imidazoleglycerol-phosphate dehydratase is an enzyme catalysing the sixth step of histidine production.

Most archaea lack ilvA, and only a limited number possess catabolic threonine dehydratase.

Serine dehydratase has also been found to be absent in human colon carcinoma and rat sarcoma.

Serine is then converted to pyruvate by serine dehydratase.

Serine Dehydratase is also known as:

ALA dehydratase deficiency is inherited in an autosomal recessive manner.

For example, serine dehydratase converts serine to pyruvate and ammonia.

L-Serine dehydratase condenses homocysteine with serine to form cystathionine.

Biosynthesis: The enzyme 3-dehydroquinate dehydratase uses 3-dehydroquinate to produce 3-dehydroshikimate and HO.

Two isomers are important, the 2- and 3-isopropyl derivatives, and these are interconverted by isopropylmalate dehydratase.

Dehydratase is an enzyme that catalyzes the removal of oxygen and hydrogen from organic compounds in the form of water.

It begins by the degradation of glycerol, a compound naturally found in wine at levels of 5-8 g/L, via a dehydratase enzyme to 3-hydroxypropionaldehyde.

In addition, researchers have shown that L-threonine competitively inhibits Serine Dehydratase as well.

Pterin-4-alpha-carbinolamine dehydratase is an enzyme that in humans is encoded by the PCBD1 gene.

As mentioned previously, two classes of 3-Dehydroquinate Dehydratase exist, known as types I and II.

Moreover, insulin is known to accelerate glycolysis and repress induction of liver serine dehydratase in adult diabetic rats.

In both Pseudomonas and Bordetella species P9 appears to be located upstream of a predicted threonine dehydratase gene.

In E. coli the enzyme encoded by the gene hisB is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase.

In overall terms, the reaction catalyzed by serine dehydratase involves two steps: catalytic elimination and a nonenzymatic hydrolysis reaction.

Studies have been conducted to show insulin causes a 40-50% inhibition of the induction serine dehydratase by glucagon in hepatocytes of rats.