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Statements

Subject Item
dbr:Amino_acid_kinase
rdf:type
yago:Family108078020 wikidata:Q8054 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity yago:Unit108189659 yago:WikicatProteinFamilies owl:Thing dbo:Protein yago:Group100031264 wikidata:Q206229 dbo:Biomolecule yago:SocialGroup107950920 yago:Abstraction100002137
rdfs:label
Amino acid kinase
rdfs:comment
In molecular biology, the amino acid kinase domain is a protein domain. It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS). In Escherichia coli, thrA, metLM, and lysC encode aspartokinase isozymes that show feedback inhibition by threonine, methionine, and lysine, respectively. The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small subunits.
dbp:name
AA_kinase
foaf:depiction
n4:PDB_2bty_EBI.jpg
dcterms:subject
dbc:Protein_families
dbo:wikiPageID
32018124
dbo:wikiPageRevisionID
997425461
dbo:wikiPageWikiLink
dbr:Aspartate dbr:Kinase dbr:Dehydrogenase dbr:Amino_acid dbc:Protein_families dbr:Leaf dbr:Amino_acids dbr:Nitrogen dbr:Lysine dbr:Aspartate_kinase dbr:Prokaryotes dbr:Threonine dbr:Aspartic_acid dbr:Plants dbr:Carbon dbr:Metabolism dbr:Arabidopsis_thaliana dbr:Isoenzyme dbr:Synthase dbr:Gene_regulation dbr:Isozymes dbr:Carbon_fixation dbr:Enzyme dbr:LysC dbr:Plant dbr:Biochemistry dbr:Glutamate dbr:Regulation dbr:Asparagine dbr:Gene_expression dbr:Protein_subunit dbr:Uridylate
owl:sameAs
yago-res:Amino_acid_kinase freebase:m.0gwz1f4 wikidata:Q83137872 n19:8Qp33
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dbt:Orphan dbt:InterPro_content dbt:Infobox_protein_family dbt:Reflist
dbo:thumbnail
n4:PDB_2bty_EBI.jpg?width=300
dbp:prosite
PDOC00289
dbp:scop
1
dbp:caption
acetylglutamate kinase from thermotoga maritima complexed with its inhibitor arginine
dbp:interpro
IPR001048
dbp:pfam
PF00696
dbp:symbol
AA_kinase
dbo:abstract
In molecular biology, the amino acid kinase domain is a protein domain. It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS). In Escherichia coli, thrA, metLM, and lysC encode aspartokinase isozymes that show feedback inhibition by threonine, methionine, and lysine, respectively. The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small subunits. In plants although the control of carbon fixation and nitrogen assimilation has been studied in detail, relatively little is known about the regulation of carbon and nitrogen flow into amino acids. The metabolic regulation of expression of an Arabidopsis thaliana aspartate kinase/homoserine dehydrogenase (AK/HSD) gene, which encodes two linked key enzymes in the biosynthetic pathway of aspartate family amino acids has been studied. The conversion of aspartate into either the storage amino acid asparagine or aspartate family amino acids may be subject to a coordinated, reciprocal metabolic control, and this biochemical branch point is a part of a larger, coordinated regulatory mechanism of nitrogen and carbon storage and utilization.
gold:hypernym
dbr:Domain
prov:wasDerivedFrom
wikipedia-en:Amino_acid_kinase?oldid=997425461&ns=0
dbo:wikiPageLength
3373
dbo:symbol
AA_kinase
foaf:isPrimaryTopicOf
wikipedia-en:Amino_acid_kinase