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Search results 201 to 217 out of 217 for Tdh

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0.021s

Type

Details

Score

Protein Domain

IPR038689 | TDH_sf

Type:

Homologous_superfamily

Description:

Thermostable direct haemolysin (TDH) is considered an important virulence factor in Vibrio parahaemolyticus gastroenteritis and is a dimer composed of two identical subunit molecules of approximately 21kDa. The tetrameric form contains a central pore permitting entry and exit of water molecules. A number of biological properties have been attributed to TDH including haemolytic activity, enterotoxicity, cytotoxicity and cardiotoxicity [].Structurally, this superfamily consists of 10 beta strands, 1 alpha helix and 1 3(10)-helix.

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Protein Domain

IPR005787 | Thr_deHydtase_biosynth

Type:

Family

Description:

Threonine dehydratase () (TDH) catalyzes the dehydratation of threonine into alpha-ketobutarate and ammonia. In Escherichia coli and other microorganisms, two classes of TDH are known to exist. One is involvedin the biosynthesis of isoleucine, the other in hydroxamino acid catabolism.This entry describes a form of threonine dehydratase with two copies of the threonine dehydratase C-terminal domain (_. Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine.

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Publication

2674117 | -

First Author:	Ogawa H
Year:	1989
Journal:	J Biol Chem
Title:	Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources.
Volume:	264
Issue:	27
Pages:	15818-23

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Publication

3540965 | -

First Author:	Datta P
Year:	1987
Journal:	Proc Natl Acad Sci U S A
Title:	Covalent structure of biodegradative threonine dehydratase of Escherichia coli: homology with other dehydratases.
Volume:	84
Issue:	2
Pages:	393-7

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Protein Domain

IPR000634 | Ser/Thr_deHydtase_PyrdxlP-BS

Type:

Binding_site

Description:

Pyridoxal phosphate is the active form of vitamin B6 (pyridoxine or pyridoxal). Pyridoxal 5'-phosphate (PLP) is a versatile catalyst, acting as a coenzyme in a multitude of reactions, including decarboxylation, deamination and transamination [, , ]. PLP-dependent enzymes are primarily involved in the biosynthesis of amino acids and amino acid-derived metabolites, but they are also found in the biosynthetic pathways of amino sugars and in the synthesis or catabolism of neurotransmitters; pyridoxal phosphate can also inhibit DNA polymerases and several steroid receptors []. Inadequate levels of pyridoxal phosphate in the brain can cause neurological dysfunction, particularly epilepsy [].PLP enzymes exist in their resting state as a Schiff base, the aldehyde group of PLP forming a linkage with the ε-amino group of an active site lysine residue on the enzyme. The α-amino group of the substrate displaces the lysine ε-amino group, in the process forming a new aldimine with the substrate. This aldimine is the common central intermediate for all PLP-catalysed reactions, enzymatic and non-enzymatic [].Serine and threonine dehydratases [, ]are functionally and structurally related pyridoxal-phosphate dependent enzymes. L-serine dehydratase () and D-serine dehydratase () catalyse the dehydratation of L-serine (respectively D-serine) into ammonia and pyruvate. Threonine dehydratase () (TDH) catalyses the dehydratation of threonine into alpha-ketobutarate and ammonia. In Escherichia coli and other microorganisms, two classes of TDH are known to exist. One is involved in the biosynthesis of isoleucine, the other in hydroxamino acid catabolism. Threonine synthase () is also a pyridoxal-phosphate enzyme, it catalyses the transformation of homoserine-phosphate into threonine. It has been shown []that threonine synthase is distantly related to the serine/threonine dehydratases. In all these enzymes, the pyridoxal-phosphate group is attached to a lysine residue.

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Protein

Q9QZX7

Organism:	Mus musculus/domesticus
Length:	339
Fragment?:	false

•

Protein

Z4YMF3

Organism:	Mus musculus/domesticus
Length:	166
Fragment?:	true

•

Protein

D3Z221

Organism:	Mus musculus/domesticus
Length:	101
Fragment?:	true

•

Protein

A8Y5D6

Organism:	Mus musculus/domesticus
Length:	113
Fragment?:	true

•

Protein

Q3UEN6

Organism:	Mus musculus/domesticus
Length:	327
Fragment?:	false

•

Publication

3098560 | -

First Author:	Parsot C
Year:	1986
Journal:	EMBO J
Title:	Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase.
Volume:	5
Issue:	11
Pages:	3013-9

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Publication

15581583 | -

First Author:	Toney MD
Year:	2005
Journal:	Arch Biochem Biophys
Title:	Reaction specificity in pyridoxal phosphate enzymes.
Volume:	433
Issue:	1
Pages:	279-87

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Publication

8690703 | -

First Author:	Hayashi H
Year:	1995
Journal:	J Biochem
Title:	Pyridoxal enzymes: mechanistic diversity and uniformity.
Volume:	118
Issue:	3
Pages:	463-73

•

Publication

15189147 | -

First Author:	Eliot AC
Year:	2004
Journal:	Annu Rev Biochem
Title:	Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Volume:	73

Pages:	383-415

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Publication

17109392 | -

First Author:	Mozzarelli A
Year:	2006
Journal:	Chem Rec
Title:	Exploring the pyridoxal 5'-phosphate-dependent enzymes.
Volume:	6
Issue:	5
Pages:	275-87

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Publication

16763894 | -

First Author:	Clayton PT
Year:	2006
Journal:	J Inherit Metab Dis
Title:	B6-responsive disorders: a model of vitamin dependency.
Volume:	29
Issue:	2-3
Pages:	317-26

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Publication

7748903 | -

First Author:	John RA
Year:	1995
Journal:	Biochim Biophys Acta
Title:	Pyridoxal phosphate-dependent enzymes.
Volume:	1248
Issue:	2
Pages:	81-96

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