Top 10 similar words or synonyms for dihydrodipicolinate

dihydropicolinate    0.862516

argj    0.813536

dehydroquinate    0.800978

dihydropteroate    0.796217

diaminopimelate    0.792638

glutamylputrescine    0.792540

cytidyltransferase    0.788522

hymidylate    0.787201

isopropylmalate    0.783504

monteralerio    0.782239

Top 30 analogous words or synonyms for dihydrodipicolinate

Article Example
Dihydrodipicolinate synthase The sequences of 4-hydroxy-tetrahydrodipicolinate synthase from different sources are well-conserved. The structure takes the form of a homotetramer, in which 2 monomers are related by an approximate 2-fold symmetry. Each monomer comprises 2 domains: an 8-fold alpha-/beta-barrel, and a C-terminal alpha-helical domain. The fold resembles that of "N"-acetylneuraminate lyase. The active site lysine is located in the barrel domain, and has access via 2 channels on the C-terminal side of the barrel.
Dihydrodipicolinate synthase This enzyme belongs to the family of lyases, specifically the amine-lyases, which cleave carbon-nitrogen bonds. 4-hydroxy-tetrahydrodipicolinate synthase is the key enzyme in lysine biosynthesis via the diaminopimelate pathway of prokaryotes, some phycomycetes, and higher plants. The enzyme catalyses the condensation of L-aspartate-beta-semialdehyde and pyruvate to 4-hydroxy-tetrahydropicolinic acid via a ping-pong mechanism in which pyruvate binds to the enzyme by forming a Schiff base with a lysine residue.
Dihydrodipicolinate synthase 4-Hydroxy-tetrahydrodipicolinate synthase (, "dihydrodipicolinate synthase", "dihydropicolinate synthetase", "dihydrodipicolinic acid synthase", "L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing)", "dapA (gene)") is an enzyme with the systematic name "L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming)". This enzyme catalyses the following chemical reaction
Dihydrodipicolinate synthase Three other proteins are structurally related to this enzyme and probably also act via a similar catalytic mechanism. These are "Escherichia coli" N-acetylneuraminate lyase () (protein NanA), which catalyses the condensation of "N"-acetyl-D-mannosamine and pyruvate to form "N"-acetylneuraminate; "Rhizobium meliloti" ("Sinorhizobium meliloti") protein MosA, which is involved in the biosynthesis of the rhizopine 3-"O"-methyl-scyllo-inosamine; and "E. coli" hypothetical protein YjhH.
Amino acid kinase 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.
Amino acid synthesis Lysine is synthesized from aspartate via the diaminopimelate (DAP) pathway. The initial two stages of the DAP pathway are catalyzed by aspartokinase and aspartate semialdehyde dehydrogenase and play a key role in the biosynthesis of lysine, threonine and methionine. There are two bifunctional aspartokinase/homoserine dehydrogenases, ThrA and MetL, in addition to a monofunctional aspartokinase, LysC. Transcription of aspartokinase genes is regulated by concentrations of the subsequently produced amino acids, lysine, threonine and methionine. The higher these amino acids concentrations, the less the gene is transcribed. ThrA and LysC are also feed-back inhibited by threonine and lysine. Finally, DAP decarboxylase LysA mediates the last step of the lysine synthesis and is common for all studied bacterial species. The formation of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is also inhibited by both lysine and threonine, which prevents the formation of the amino acids derived from aspartate. Additionally, high lysine concentrations inhibit the activity of dihydrodipicolinate synthase (DHPS). So, in addition to inhibiting the first enzyme of the aspartate families biosynthetic pathway, lysine also inhibits the activity of the first enzyme after the branch point, i.e. the enzyme that is specific for lysine’s own synthesis.