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Search results 401 to 433 out of 433 for Ak2

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Type Details Score
Publication
9434148 | J:44883
First Author: Noma T
Year: 1998
Journal: Biochim Biophys Acta
Title: cDNA cloning and tissue-specific expression of the gene encoding human adenylate kinase isozyme 2.
Volume: 1395
Issue: 1
Pages: 34-9
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Protein Domain
IPR018042 | Aspartate_kinase_CS
Type: Conserved_site
Description: Aspartate kinase () (AK) catalyzes the first reaction in the aspartate pathway; the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine [].In bacteria there are three different aspartate kinase isozymes which differ in sensitivity to repression and inhibition by Lys, Met and Thr. AK1 and AK2 are bifunctional enzymes which both consist of an N-terminal AK domain and a C-terminal homoserine dehydrogenase domain. AK1 is involved in threonine biosynthesis and AK2, in that of methionine. The third isozyme, AK3 is monofunctional and involved in lysine synthesis. In archaea and plants there may be a single isozyme of AK which in plants is multifunctional.This entry represents a region encoding aspartate kinase activity found in both the monofunctional and bifunctional enzymes.Synonym(s): Aspartokinase
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Publication
12888214 | J:86031
First Author: Du X
Year: 2003
Journal: Brain Res Dev Brain Res
Title: Identity and neuroanatomical localization of messenger RNAs that change expression in the neural tube of mouse embryos within 1 h after ethanol exposure.
Volume: 144
Issue: 1
Pages: 9-23
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Publication
2892836 | -
First Author: Rafalski JA
Year: 1988
Journal: J Biol Chem
Title: Structure of the yeast HOM3 gene which encodes aspartokinase.
Volume: 263
Issue: 5
Pages: 2146-51
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Publication
9813319 | J:51041
First Author: Yoneda T
Year: 1998
Journal: Brain Res Mol Brain Res
Title: Identification of a novel adenylate kinase system in the brain: cloning of the fourth adenylate kinase.
Volume: 62
Issue: 2
Pages: 187-95
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Publication
218813 | -
First Author: Tomasselli AG
Year: 1979
Journal: Eur J Biochem
Title: Mitochondrial GTP-AMP phosphotransferase. 2. Kinetic and equilibrium dialysis studies.
Volume: 93
Issue: 2
Pages: 263-7
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Publication
6088234 | -
First Author: Wieland B
Year: 1984
Journal: Eur J Biochem
Title: The amino acid sequence of GTP:AMP phosphotransferase from beef-heart mitochondria. Extensive homology with cytosolic adenylate kinase.
Volume: 143
Issue: 2
Pages: 331-9
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Publication
1587477 | -
First Author: Cooper AJ
Year: 1992
Journal: Gene
Title: A putative second adenylate kinase-encoding gene from the yeast Saccharomyces cerevisiae.
Volume: 114
Issue: 1
Pages: 145-8
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Protein Domain
IPR000850 | Adenylat/UMP-CMP_kin
Type: Family
Description: Adenylate kinases (ADK) are phosphotransferases that catalyse the reversible reaction AMP + MgATP = ADP + MgADPan essential reaction for many processes in living cells. Two ADK isozymes have been identified in mammalian cells. These specifically bind AMP and favour binding to ATP over other nucleotide triphosphates (AK1 is cytosolic and AK2 is located in the mitochondria). A third ADK has been identified in bovine heart and human cells [], this is a mitochondrial GTP:AMP phosphotransferase, also specific for the phosphorylation of AMP, but can only use GTP or ITP as asubstrate []. ADK has also been identified in different bacterial species and in yeast []. Two further enzymes are known to be related to the ADK family, i.e. yeast uridine monophosphokinase and slime mold UMP-CMP kinase. Within the ADK family there are several conserved regions, including the ATP-binding domains. One of the most conserved areas includes an Arg residue, whose modification inactivates the enzyme, together with an Asp that resides in the catalytic cleft of the enzyme and participates in a salt bridge.In humans, nine different AK isoenzymes have been identified (AK1-9) [].
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Protein Domain
IPR001341 | Asp_kinase
Type: Domain
Description: Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids - lysine, threonine, methionine and isoleucine - in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential component of bacterial cell wall biosynthesis, and dipicolinic acid, which is involved in sporulation in Gram-positive bacteria. Members of the animal kingdom do not posses this pathway and must therefore acquire these essential amino acids through their diet. Research into improving the metabolic flux through this pathway has the potential to increase the yield of the essential amino acids in important crops, thus improving their nutritional value. Additionally, since the enzymes are not present in animals, inhibitors of them are promising targets for the development of novel antibiotics and herbicides. For more information see [].Aspartate kinase () (AK) catalyzes the first reaction in the aspartate pathway; the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine [].In bacteria there are three different aspartate kinase isozymes which differ in sensitivity to repression and inhibition by Lys, Met and Thr. AK1 and AK2 are bifunctional enzymes which both consist of an N-terminal AK domain and a C-terminal homoserine dehydrogenase domain. AK1 is involved in threonine biosynthesis and AK2, in that of methionine. The third isozyme, AK3 is monofunctional and involved in lysine synthesis. In archaea and plants there may be a single isozyme of AK which in plants is multifunctional.
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Protein
F7BP55
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: true
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Protein
Z4YN97
Organism: Mus musculus/domesticus
Length: 89  
Fragment?: true
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Protein
Q9D2H2
Organism: Mus musculus/domesticus
Length: 614  
Fragment?: false
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Protein
Q920P5
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Protein
Q9DBP5
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: false
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Protein
Q32M07
Organism: Mus musculus/domesticus
Length: 479  
Fragment?: false
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Protein
A0A0G2JGN7
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
A0A0R4J093
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
A2ARF5
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: true
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Protein
F8WIC0
Organism: Mus musculus/domesticus
Length: 723  
Fragment?: false
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Protein
A0A1B0GRV7
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
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Protein
A2ARF6
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Protein
A0A0A6YXW8
Organism: Mus musculus/domesticus
Length: 96  
Fragment?: true
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Protein
G3UYQ4
Organism: Mus musculus/domesticus
Length: 1894  
Fragment?: false
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Protein
Q9R0Y5
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
Q9D8W6
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
F6RP11
Organism: Mus musculus/domesticus
Length: 65  
Fragment?: true
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Protein
Q9WTP7
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
Q9WUR9
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
Q3UYL0
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: true
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Protein
Q3U489
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
F6TEU8
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: true
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Publication
11352712 | -
First Author: Viola RE
Year: 2001
Journal: Acc Chem Res
Title: The central enzymes of the aspartate family of amino acid biosynthesis.
Volume: 34
Issue: 5
Pages: 339-49
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