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Information on EC 2.3.3.14 - homocitrate synthase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession Q4J989

for references in articles please use BRENDA:EC2.3.3.14
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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.3 Acyl groups converted into alkyl groups on transfer
                2.3.3.14 homocitrate synthase
IUBMB Comments
Belongs in the alpha-aminoadipate pathway of lysine synthesis, along with EC 4.2.1.36, homoaconitate hydratase. The enzyme also acts with oxaloacetate as substrate, but more slowly [2,3].
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This record set is specific for:
Sulfolobus acidocaldarius
UNIPROT: Q4J989
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Word Map
  • 2.3.3.14
  • gyrus
  • resting-state
  • frontal
  • deficit
  • sclerosis
  • cingulate
  • schizophrenia
  • hair
  • emotional
  • prefrontal
  • inferior
  • anxiety
  • bipolar
  • neuropsychological
  • auditory
  • parietal
  • insula
  • neuroimaging
  • occipital
  • default
  • precuneus
  • high-content
  • verbal
  • cochlea
  • putamen
  • whole-brain
  • tensor
  • voxel-based
  • precentral
  • nervosa
  • first-episode
  • relapsing-remitting
  • obsessive-compulsive
  • salience
  • hemichannels
  • t1-weighted
  • orbitofrontal
  • dlpfc
  • visuospatial
  • unmedicated
  • parahippocampal
  • impulsivity
  • event-related
  • fluency
  • fasciculus
  • connectome
  • tractography
  • peripapillary
  • euthymic
  • stroop
  • biotechnology
  • synthesis
  • medicine
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hcs, homocitrate synthase, lys22, nifv2, sphcs, tthcs, lys21p, homocitrate synthetase, lys22p, saci_1304, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating)
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-
-
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acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase
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-
-
-
HCS
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-
-
-
homocitrate synthetase
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-
-
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homocitrate-condensing enzyme
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-
-
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homocondensing enzyme
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-
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synthase, homocitrate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl forming)
Belongs in the alpha-aminoadipate pathway of lysine synthesis, along with EC 4.2.1.36, homoaconitate hydratase. The enzyme also acts with oxaloacetate as substrate, but more slowly [2,3].
CAS REGISTRY NUMBER
COMMENTARY hide
9075-60-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
show the reaction diagram
the enzyme catalyzes the first and committed step of the alpha-aminoadipate pathway
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lysine
mutant enzyme lacking the RAM domain is insensitive to inhibition by lysine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the first and committed step of the alpha-aminoadipate pathway
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the RAM domain is responsible for enzyme inhibition. A mutant enzyme lacking the RAM domain is insensitive to inhibition by lysine
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suzuki, T.; Akiyama, N.; Yoshida, A.; Tomita, T.; Lassak, K.; Haurat, M.F.; Okada, T.; Takahashi, K.; Albers, S.V.; Kuzuyama, T.; Nishiyama, M.
Biochemical characterization of archaeal homocitrate synthase from Sulfolobus acidocaldarius
FEBS Lett.
594
126-134
2020
Sulfolobus acidocaldarius (Q4J989), Sulfolobus acidocaldarius DSM 639 (Q4J989)
Manually annotated by BRENDA team