1.1.1.3: homoserine dehydrogenase
This is an abbreviated version!
For detailed information about homoserine dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.3
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1.1.1.3
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l-threonine
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threonine-sensitive
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corynebacterium
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glutamicum
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l-lysine
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semialdehyde
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dihydrodipicolinate
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l-isoleucine
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brevibacterium
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aspartate-derived
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2.7.2.4
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i-homoserine
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rhodospirillum
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lysine-sensitive
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lactofermentum
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feedback-insensitive
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feedback-resistant
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synthesis
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drug development
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agriculture
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pharmacology
- 1.1.1.3
- l-threonine
-
threonine-sensitive
- corynebacterium
- glutamicum
- l-lysine
- semialdehyde
- dihydrodipicolinate
- l-isoleucine
- brevibacterium
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aspartate-derived
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2.7.2.4
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i-homoserine
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rhodospirillum
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lysine-sensitive
- lactofermentum
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feedback-insensitive
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feedback-resistant
- synthesis
- drug development
- agriculture
- pharmacology
Reaction
Synonyms
AK-HDH, AK-HSD-1, AK-HSDH, AK-HseDH, aspartate kinase-homoserine dehydrogenase, aspartokinase-homoserine dehydrogenase I, bifunctional aspartate kinase-homoserine dehydrogenase, BsHSD, HDH, hom, hom-1, Hom6, homoserine dehydrogenase 1, homoserine dehydrogenase 2, HSD, HSDH, HseDH, More, orf19.2951, PbHSD, SACOL1362, StHSD, thrA, TM_0547, TTHA0489, TtHSD
ECTree
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Subunits
Subunits on EC 1.1.1.3 - homoserine dehydrogenase
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dimer
homodimer
homopentamer or homohexamer
tetramer
additional information
dimer
StHSD is composed of a nucleotide-binding region (residues 1-130 and 285-304), a dimerization region (residues 131-145 and 256-284), and a catalytic region (residues 146-255). Presence of a disulfide bond formed between two cysteine residues (position 304) in the C-terminal regions of the two subunits
dimer
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StHSD is composed of a nucleotide-binding region (residues 1-130 and 285-304), a dimerization region (residues 131-145 and 256-284), and a catalytic region (residues 146-255). Presence of a disulfide bond formed between two cysteine residues (position 304) in the C-terminal regions of the two subunits
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homodimer
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2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE
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homodimer
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
homodimer
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the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
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homodimer
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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dimeric enzyme structure, overview
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x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
homopentamer or homohexamer
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x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
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homopentamer or homohexamer
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x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
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homopentamer or homohexamer
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x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
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tetramer
4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE
tetramer
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4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE
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primary and secondary structure comparison, the bifunctional enzyme contains 2 homologous subdomains defined by a common loop-alpha helix-loop-beta strand-loop-beta strand motif, the enzymes' regulatory domain is composed of 2 subdomains, amino acid residues 414-453 and 495-534
additional information
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
additional information
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the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
additional information
-
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
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additional information
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview
additional information
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structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview
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additional information
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
additional information
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structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
additional information
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structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
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additional information
enzyme TtHSD folds into a dimer with a noncrystallographic 2fold axis. The subunit comprises three conserved domains of HSDs and a flexible tail at the C-terminus. The nucleotide-binding domain (residues 1-119 and 288-309) assumes an alpha/beta Rossmann fold with five beta-strands and four alpha-helices. The dimerization domain (residues 120-140 and 261-287) comprises two alpha-helices and two beta-strands that interact with the corresponding domain of the other subunit of the dimer to form an alpha/beta structure with the four-stranded beta-sheet. The substrate-binding domain (residues 141-260) comprises four beta-strands and five alpha-helices. The flexible tail at the C-terminus (310-332) extends from the nucleotide-binding domain to the substrate-binding domain
additional information
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enzyme TtHSD folds into a dimer with a noncrystallographic 2fold axis. The subunit comprises three conserved domains of HSDs and a flexible tail at the C-terminus. The nucleotide-binding domain (residues 1-119 and 288-309) assumes an alpha/beta Rossmann fold with five beta-strands and four alpha-helices. The dimerization domain (residues 120-140 and 261-287) comprises two alpha-helices and two beta-strands that interact with the corresponding domain of the other subunit of the dimer to form an alpha/beta structure with the four-stranded beta-sheet. The substrate-binding domain (residues 141-260) comprises four beta-strands and five alpha-helices. The flexible tail at the C-terminus (310-332) extends from the nucleotide-binding domain to the substrate-binding domain