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Information on EC 4.1.3.4 - hydroxymethylglutaryl-CoA lyase and Organism(s) Bacillus subtilis and UniProt Accession O34873

for references in articles please use BRENDA:EC4.1.3.4
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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.4 hydroxymethylglutaryl-CoA lyase
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Select one or more organisms in this record:
This record set is specific for:
Bacillus subtilis
UNIPROT: O34873 not found.
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Bacillus subtilis
Synonyms
3-hydroxy-3-methylglutarate-CoA lyase, 3-Hydroxy-3-methylglutaryl CoA cleaving enzyme, 3-hydroxy-3-methylglutaryl CoA lyase, 3-Hydroxy-3-methylglutaryl coenzyme A lyase, 3-Hydroxy-3-methylglutaryl-CoA lyase, 3-hydroxy-3-methylglutaryl-CoA lyase-like protein, 3-hydroxy-3-methylglutaryl-coenzyme A lyase, 3-hydroxy-methylglutaryl coenzyme A lyase, beta-hydroxy-beta-methylglutaryl-CoA lyase, HCL1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxy-3-methylglutarate-CoA lyase
3-Hydroxy-3-methylglutaryl CoA cleaving enzyme
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3-Hydroxy-3-methylglutaryl coenzyme A lyase
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3-Hydroxy-3-methylglutaryl-CoA lyase
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HMG CoA cleavage enzyme
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HMG-CoA lyase
Hydroxymethylglutaryl coenzyme A lyase
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Hydroxymethylglutaryl coenzyme A-cleaving enzyme
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SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase (acetyl-CoA-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-83-5
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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
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
can replace Mn2+ required for activity
Mn2+
required for activity
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
static light scattering, crystal contains two dimers forming a pseudotetramer per asymmetric unit
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method; hanging drop vapour diffusion method with 22.5% (w/v) PEG 3350, 210 mM sodium iodide, 5 mM EDTA, 10 mM dithiothreitol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C240A
increased Km relative to the wild type enzyme
C240S
decreased Km relative to the wild type enzyme
D16E
decreased Km relative to the wild type enzyme
D16N
decreased Km relative to the wild type enzyme
D178A
increased Km relative to the wild type enzyme
D254A
decreased Km relative to the wild type enzyme
E11D
decreased Km relative to the wild type enzyme
E253A
decreased Km relative to the wild type enzyme
E46A
increased Km relative to the wild type enzyme
H207A
increased Km relative to the wild type enzyme
H207D
increased Km relative to the wild type enzyme
H207R
decreased Km relative to the wild type enzyme
K297S
increased Km relative to the wild type enzyme
R15Q
increased Km relative to the wild type enzyme
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
; nickel-nitrilotriacetic acid column chromatography and Superdex 75 gel filtration
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
mutations in this enzyme cause a human autosomal recessive disorder called primary metabolic aciduria
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Forouhar, F.; Hussain, M.; Farid, R.; Benach, J.; Abashidze, M.; Edstrom, W.C.; Vorobiev, S.M.; Xiao, R.; Acton, T.B.; Fu, Z.; Kim, J.J.; Miziorko, H.M.; Montelione, G.T.; Hunt, J.F.
Crystal structures of two bacterial Hmg-CoA lyases suggest a common catalytic mechanism among a family of TIM-barrel metalloenzymes cleaving carbon-carbon bonds
J. Biol. Chem.
281
7533-7545
2005
Bacillus subtilis, Bacillus subtilis (O34873), Brucella melitensis, Brucella melitensis (Q8YEF2)
Manually annotated by BRENDA team
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