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Information on EC 4.1.3.4 - hydroxymethylglutaryl-CoA lyase and Organism(s) Homo sapiens
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4.1.3.4 hydroxymethylglutaryl-CoA lyaseSpecify your search results
Word Map
- 4.1.3.4
-
3-hydroxy-3-methylglutaric
- aciduria
-
ketogenesis
- hypoglycemia
- acidosis
-
inborn
-
3-methylglutaric
-
3-methylglutaconic
-
ketogenic
-
3-hydroxyisovaleric
-
hyperammonemia
-
hypoketotic
- mevalonii
- lethargy
- 3-methylcrotonyl-coa
- medicine
- acetoacetyl-coa
-
hl-deficient
- hmgcs2
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hmg-coa lyase, hmgcl, 3-hydroxy-3-methylglutaryl-coa lyase, hmgcll1, 3-hydroxy-3-methylglutaryl-coenzyme a lyase, 3-hydroxy-3-methylglutaryl coenzyme a lyase, hydroxymethylglutaryl-coa lyase, 3-hydroxy-3-methylglutaryl coa lyase, hmg coa lyase, liue protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy-3-methylglutarate-CoA lyase
3-Hydroxy-3-methylglutaryl CoA cleaving enzyme
-
-
-
-
3-Hydroxy-3-methylglutaryl coenzyme A lyase
-
-
-
-
3-Hydroxy-3-methylglutaryl-CoA lyase
HMG CoA cleavage enzyme
-
-
-
-
HMG-CoA lyase
Hydroxymethylglutaryl coenzyme A lyase
-
-
-
-
Hydroxymethylglutaryl coenzyme A-cleaving enzyme
-
-
-
-
3-hydroxy-3-methylglutarate-CoA lyase
-
-
-
-
3-Hydroxy-3-methylglutaryl-CoA lyase
-
-
-
-
HMG-CoA lyase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-3-Hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate
identification of reactive cysteines, possibly regulatory mechanism via thiol/disulfide exchange
-
(S)-3-Hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate
identification of functionally important S69
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase (acetyl-CoA-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9030-83-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
-
involved in ketogenesis, leucine catabolism
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
-
involved in ketogenesis, leucine catabolism
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
-
identification of His233, His235, ASp42, and Asn275 as metal-binding ligands
Mg2+
-
required, Km for wild-type HMGCL is 0.233 mM and for HMGCL mutant C323A 0.322 mM
Mg2+
-
required, Km of wild-type HMGCLL1 is 0.049 mM and for HMGCLL1 mutant G2A 0.088 mM
Mn2+
-
required, Km for wild-type HMGCL is 0.00034 mM and for HMGCL mutant C323A 0.00037 mM
Mn2+
-
required, Km of wild-type HMGCLL1 is 0.00018 mM and for HMGCLL1 mutant G2A 0.00024 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-epigallocatechin gallate
-
a mixed-type noncompetitive inhibitor, contribution of the gallyl moiety, which forms a hexa-coordination complex with the Mg2+ ion, to enzymatic inhibition
additional information
-
C323 involved in intersubunit cross-linking upon oxidative inactivation, thiol-disulfide exchange mechanism
-
additional information
-
no inhibition by daidzein, hesperetin, naringenin, (+)-catechin, and (-)-epicatechin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.024
(S)-3-hydroxy-3-methylglutaryl-CoA
-
HMGCLL1 mutant G2A and wild-type HMGCL, pH 8.2, 37°C
0.0134
3-hydroxy-3-methylglutaryl-CoA
-
K48Q mutant protein, pH not specified in the publication, 30°C
0.0209
3-hydroxy-3-methylglutaryl-CoA
-
K48N mutant protein, pH not specified in the publication, 30°C
0.026
3-hydroxy-3-methylglutaryl-CoA
pH not specified in the publication, temperature not specified in the publication
0.0265
3-hydroxy-3-methylglutaryl-CoA
-
wild type protein, pH not specified in the publication, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.123
C170S/C266S mutant protein, pH not specified in the publication, temperature not specified in the publication
0.224
C266S mutant protein, pH not specified in the publication, temperature not specified in the publication
1.06
C170S/C174S mutant protein, pH not specified in the publication, temperature not specified in the publication
123
wild type protein, pH not specified in the publication, temperature not specified in the publication
128
C234S mutant protein, pH not specified in the publication, temperature not specified in the publication
132
159
18.5
C170S/C323S mutant protein, pH not specified in the publication, temperature not specified in the publication
21.2
C197S mutant protein, pH not specified in the publication, temperature not specified in the publication
348
42
C141S mutant protein, pH not specified in the publication, temperature not specified in the publication
42.1
C174S mutant protein, pH not specified in the publication, temperature not specified in the publication
53.1
C170S mutant protein, pH not specified in the publication, temperature not specified in the publication
additional information
132
C307S mutant protein, pH not specified in the publication, temperature not specified in the publication
132
C323S mutant protein, pH not specified in the publication, temperature not specified in the publication
additional information
-
enzyme activities from various enzyme deficiency patients and control individuals
additional information
-
128.86 nmol/min/g of wet weight liver tissue, 58.49 nmol/min/g of wet weight pancreas tissue, 42.48 nmol/min/g of wet weight kidney tissue, 20.23 nmol/min/g of wet weight testis tissue, 12.6 nmol/min/g of wet weight skeletal muscle, activity not detected in heart and brain
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
E37X is a common HMGCL mutation in Portuguese patients with 3-hydroxy-3-methylglutaric CoA lyase deficiency
-
-
Spanish patients with the Mediterranean nonsense mutation G109T. The mutation can produce aberrant splicing with three mRNA variants: one of the expected size, the second with deletion of exon 2, and the third with deletion of exons 2 and 3
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
HMGCLL1 is overexpressed in certain types of human brain cancer cells
additional information
additional information
-
tissue distribution of 3-hydroxy-3-methylglutaryl-CoA lyase, overview
additional information
-
tissue distribution of 3-hydroxy-3-methylglutaryl-CoA lyase-like protein, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
wild-type 3-hydroxy-3-methylglutaryl-CoA lyase-like protein, myristoylation dependent association with nonmitochondrial membrane compartments
-
additional information
-
enzyme differs from mitochondrial enzyme according to immunoreactivity and other properties, mitochondrial leader sequence influences quaternary structure
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
-
the enzyme is a rate-limiting enzyme in hepatic cells catalyzing the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetate
malfunction
-
3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency is an inborn error of metabolism characterized by impairment of ketogenesis and leucine catabolism resulting in an organic acidopathy
malfunction
-
3-Hydroxy-3-methylglutaric aciduria is a rare human autosomal recessive disorder caused by deficiency of 3-hydroxy-3-methylglutaryl CoA lyase
malfunction
-
inhibition of this enzyme results in reduced acetoacetate production and impaired ketoacidosis. High levels of secreted ketone bodies (acetoacetate and 3beta-hydroxybutyrate) lower the pH of blood and urine, resulting in ketoacidosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HMGC2_HUMAN
370
0
39514
Swiss-Prot
other Location (Reliability: 2)
HMGCL_HUMAN
325
0
34360
Swiss-Prot
Mitochondrion (Reliability: 1)
O95896_HUMAN
191
0
20208
TrEMBL
other Location (Reliability: 1)
Q9NT06_HUMAN
157
0
16899
TrEMBL
other Location (Reliability: 3)
H0Y2L7_HUMAN
182
0
19081
TrEMBL
Mitochondrion (Reliability: 2)
G5E9S9_HUMAN
151
0
16445
TrEMBL
other Location (Reliability: 3)
B7Z212_HUMAN
237
0
25204
TrEMBL
other Location (Reliability: 3)
B1AK13_HUMAN
300
0
31735
TrEMBL
other Location (Reliability: 4)
B7Z4D4_HUMAN
174
0
18527
TrEMBL
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31600
32000
34100
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
-
X-ray crystallography, the hexamer consists of three dimers which are supposed to be the physiological enzyme form in solution
tetramer
-
analytical ultracentrifugation, enzyme exists as a mixture of dimers and tetramers
additional information
-
C323 involved in intersubunit cross-linking upon oxidative inactivation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
the deduced 3-hydroxy-3-methylglutaryl-CoA lyase-like protein, HMGCLL1, sequence contains an N-terminal myristoylation motif. Myristoylation of HMGCLL1 affects its cellular localization
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.1 A resolution of the recombinant mitochondrial HMG-CoA lyase containing a bound activator cation and 3-hydroxyglutarate. For crystallization experiments, the enzyme is diluted to 5 6 mg/ml. The competitive inhibitor hydroxyglutaryl-CoA is added to the diluted protein at about 1mM concentration. The inhibitor is necessary for generation of uniform diffraction quality crystals. Crystals sufficient for X-ray studies are obtained using an equilibration buffer of 0.1 M Hepes, pH 7.5, 60 mM MgCl2,and 15% polyethylene glycol 8K. The enzyme is mixed 1:1 with the equilibration buffer using sitting drop trays at 19°C. Crystals belong to the monoclinic space group C2 with unit cell parameters a = 197.0 A, b = 117.1 A, c = 86.8 A, and beta = 112.5°. Six monomers are found in the asymmetric unit
-
sitting drop vapour diffusion method with 0.1 M HEPES, pH 7.5, 60 mM MgCl2, and 15% polyethylene glycol 8K
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C141S
strong inter-subunit dimer formation (SDS-PAGE, non-reducing conditions)
C170S
inter-subunit dimer formation not observed (SDS-PAGE, non-reducing conditions)
C170S/C174S
moderate inter-subunit dimer formation (SDS-PAGE, non-reducing conditions)
C170S/C266S
inter-subunit dimer formation not observed (SDS-PAGE, non-reducing conditions)
C170S/C323S
inter-subunit dimer formation not observed (SDS-PAGE, non-reducing conditions)
C174S
moderate inter-subunit dimer formation (SDS-PAGE, non-reducing conditions)
C197S
weak inter-subunit dimer formation (SDS-PAGE, non-reducing conditions)
C234S
weak inter-subunit dimer formation (SDS-PAGE, non-reducing conditions)
C266S
inter-subunit dimer formation not observed (SDS-PAGE, non-reducing conditions)
C307S
moderate inter-subunit dimer formation (SDS-PAGE, non-reducing conditions)
C323S
D204N
D42A
D42H
E279K
E37X
-
E37X is a common HMGCL mutation in Portuguese patients with 3-hydroxy-3-methylglutaric CoA lyase deficiency
G109T
-
Spanish patients with the Mediterranean nonsense mutation G109T. The mutation can produce aberrant splicing with three mRNA variants: one of the expected size, the second with deletion of exon 2, and the third with deletion of exons 2 and 3
G203E
G2A
-
site-directed mutagenesis of HMGCLL1, eliminatin of N-terminal myristoylation motif by construction of a 3-hydroxy-3-methylglutaryl-CoA lyase-like protein HMGCLL1 G2A mutant, the mutant shows reduced activity compared to wild-type HMGCLL1
H233A
H233R
K48N
R41M
R41Q
S201Y
S75R
additional information
C323S
inter-subunit dimer formation not observed (SDS-PAGE, non-reducing conditions)
C323S
-
site-directed mutagenesis of HMGCL, the mutant shows 2fold increased activity compared to wild-type HMGCL
D204N
-
reduced catalytic efficiency, mutation causes 3-hydroxy-3-methylgluratic aciduria in vivo
G203E
the mutation causes 3-hydroxy-3-methylglutaric aciduria, it has less than 0.02% of the wild type enzyme activity
K48N
the mutation causes 3-hydroxy-3-methylglutaric aciduria, shows less than 2% of wild type HMG-CoA lyase activity
S201Y
-
no catalytic efficiency, mutation causes 3-hydroxy-3-methylgluratic aciduria in vivo
S75R
-
no catalytic efficiency, mutation causes 3-hydroxy-3-methylgluratic aciduria in vivo
additional information
the deletion mutant Mut15 (last 15 C-terminal residues deleted) shows less than 2% specific activity, the deletion mutant Mut12 (last 12 C-terminal residues deleted) shows 17% specific activity, the deletion mutant Mut9 (last 9 C-terminal residues deleted) shows 99% specific activity, the deletion mutant Mut6 (last 6 C-terminal residues deleted) shows 93% specific activity, the deletion mutant Mut3 (last 3 C-terminal residues deleted) shows 88% specific activity, compared to the wild type enzyme, respectively
additional information
-
the deletion mutant Mut15 (last 15 C-terminal residues deleted) shows less than 2% specific activity, the deletion mutant Mut12 (last 12 C-terminal residues deleted) shows 17% specific activity, the deletion mutant Mut9 (last 9 C-terminal residues deleted) shows 99% specific activity, the deletion mutant Mut6 (last 6 C-terminal residues deleted) shows 93% specific activity, the deletion mutant Mut3 (last 3 C-terminal residues deleted) shows 88% specific activity, compared to the wild type enzyme, respectively
additional information
-
c.494G to T, p.Arg165Gln, missense mutation in the 3-hydroxy-3-methylglutaryl CoA lyase gene
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is sensitive to oxidation, showing higher activity in reducing conditions
681959
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography, phenyl-agarose column chromatography, and Superose 12 column chromatography
-
recombinant active wild-type 3-hydroxy-3-methylglutaryl-CoA lyase-like protein and its mutant G2A from Pichia pastoris by nickel affinity chromatography and ultrafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of 3-hydroxy-3-methylglutaryl-CoA lyase-like protein, sequence comparison of HMGCLL1 and HMGCL, expression of 3-hydroxy-3-methylglutaryl-CoA lyase-like protein mutant G2A in COS-1 cell cytosol, recombinant expression of wild-type 3-hydroxy-3-methylglutaryl-CoA lyase-like protein in Escherichia coli and Pichia pastoris, in insoluble form
-
nucleotide sequence, identification of a 2-base pair deletion in S69 codon of enzyme-deficient patients
-
sequence comparison of HMGCLL1 and HMGCL, expression of 3-hydroxy-3-methylglutaryl-CoA lyase wild-type in COS-1 cell cytosol, recombinant expression of wild-type 3-hydroxy-3-methylglutaryl-CoA lyase in Escherichia coli and Pichia pastoris, in active form
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
genetically heterogeneous deficiency, participation of S69 codon 2-base pair deletion in some cases
medicine
-
3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency may cause hypoglycaemia which can lead to death
medicine
-
3-hydroxy-3-methylglutaryl CoA lyase deficiency is a rare autosomal recessive mitochondrial disease characterized by a deficiency in the enzyme 3-hydroxy-3-methylglutaryl CoA lyase
medicine
-
3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency is a rare inborn error affecting leucine catabolism and ketogenesis, usually presenting in the neonatal period
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wysocki, S.J.; Haehnel, R.
3-Hydroxy-3-methylglutaryl-coenzyme A lyase deficiency: a review
J. Inherit. Metab. Dis.
9
225-233
1986
Homo sapiens
Ashmarina, L.I.; Robert, M.F.; Elsliger, M.A.; Mitchell, G.A.
Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria
Biochem. J.
315
71-75
1996
Homo sapiens
Mitchell, G.A.; Robert, M.F.; Hruz, P.W.; Wang, S.; Fontaine, G.; Behnke, C.E.; Mende-Mueller, L.M.; Schappert, K.; Lee, C.; Gibson, K.M.; Miziorko, H.M.
3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL)
J. Biol. Chem.
268
4376-4381
1993
Gallus gallus, Homo sapiens
Roberts, J.R.; Narasimhan, C.; Hruz, P.W.; Mitchell, G.A.; Miziorko, H.M.
3-Hydroxy-3-methylglutaryl-CoA lyase: expression and isolation of the recombinant human enzyme and investigation of a mechanism for regulation of enzyme activity
J. Biol. Chem.
269
17841-17846
1994
Homo sapiens
Wanders, R.J.A.; Schutgens, R.B.H.; Zoeters, P.H.M.
3-Hydroxy-3-methylglutaryl-CoA lyase in human skin fibroblasts: study of its properties and deficient activity in 3-hydroxy-3-methylglutaric aciduria patients using a simple spectrophotometric method
Clin. Chim. Acta
171
95-102
1988
Homo sapiens
Tuinstra, R.L.; Burgner, J.W.2nd.; Miziorko, H.M.
Investigation of the oligomeric status of the peroxisomal isoform of human 3-hydroxy-3-methylglutaryl-CoA lyase
Arch. Biochem. Biophys.
408
286-294
2002
Homo sapiens
Tuinstra, R.L.; Wang, C.Z.; Mitchell, G.A.; Miziorko, H.M.
Evaluation of 3-hydroxy-3-methylglutaryl-coenzyme A lyase arginine-41 as a catalytic residue: Use of acetyldithio-coenzyme A to monitor product enolization
Biochemistry
43
5287-5295
2004
Homo sapiens
Casals, N.; Gomez-Puertas, P.; Pie, J.; Mir, C.; Roca, R.; Puisac, B.; Aledo, R.; Clotet, J.; Menao, S.; Serra, D.; Asins, G.; Till, J.; Elias-Jones, A.C.; Cresto, J.C.; Chamoles, N.A.; Abdenur, J.E.; Mayatepek, E.; Besley, G.; Valencia, A.; Hegardt, F.G.
Structural (betaalpha)8 TIM barrel model of 3-hydroxy-3-methylglutaryl-coenzyme A lyase
J. Biol. Chem.
278
29016-29023
2003
Homo sapiens
Ashmarina, L.I.; Pshezhetsky, A.V.; Branda, S.S.; Isaya, G.; Mitchell, G.A.
3-Hydroxy-3-methylglutaryl coenzyme A lyase: targeting and processing in peroxisomes and mitochondria
J. Lipid Res.
40
70-75
1999
Homo sapiens
Puisac, B.; Lopez-Vinas, E.; Moreno, S.; Mir, C.; Perez-Cerda, C.; Menao, S.; Lluch, D.; Pie, A.; Gomez-Puertas, P.; Casals, N.; Ugarte, M.; Hegardt, F.; Pie, J.
Skipping of exon 2 and exons 2 plus 3 of HMG-CoA lyase (HL) gene produces the loss of beta sheets 1 and 2 in the recently proposed (beta-alpha)8 TIM barrel model of HL
Biophys. Chem.
115
241-245
2005
Homo sapiens
Fu, Z.; Runquist, J.A.; Forouhar, F.; Hussain, M.; Hunt, J.F.; Miziorko, H.M.; Kim, J.J.
Crystal structure of human HMG-CoA lyase: Insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria
J. Biol. Chem.
281
7526-7532
2005
Homo sapiens
Cardoso, M.L.; Rodrigues, M.R.; Leao, E.; Martins, E.; Diogo, L.; Rodrigues, E.; Garcia, P.; Rolland, M.O.; Vilarinho, L.
The E37X is a common HMGCL mutation in Portuguese patients with 3-hydroxy-3-methylglutaric CoA lyase deficiency
Mol. Genet. Metab.
82
334-338
2004
Homo sapiens
Al-Sayed, M.; Imtiaz, F.; Alsmadi, O.A.; Rashed, M.S.; Meyer, B.F.
Mutations underlying 3-hydroxy-3-methylglutaryl CoA lyase deficiency in the Saudi population
BMC Med. Genet.
7
86
2006
Homo sapiens
Mir, C.; Lopez-Vinas, E.; Aledo, R.; Puisac, B.; Rizzo, C.; Dionisi-Vici, C.; Deodato, F.; Pie, J.; Gomez-Puertas, P.; Hegardt, F.G.; Casals, N.
A single-residue mutation, G203E, causes 3-hydroxy-3-methylglutaric aciduria by occluding the substrate channel in the 3D structural model of HMG-CoA lyase
J. Inherit. Metab. Dis.
29
64-70
2006
Homo sapiens (P35914)
Carrasco, P.; Menao, S.; Lopez-Vinas, E.; Santpere, G.; Clotet, J.; Sierra, A.Y.; Gratacos, E.; Puisac, B.; Gomez-Puertas, P.; Hegardt, F.G.; Pie, J.; Casals, N.
C-terminal end and amino acid Lys48 in HMG-CoA lyase are involved in substrate binding and enzyme activity
Mol. Genet. Metab.
91
120-127
2007
Homo sapiens (P35914), Homo sapiens
Pie, J.; Lopez-Vinas, E.; Puisac, B.; Menao, S.; Pie, A.; Casale, C.; Ramos, F.J.; Hegardt, F.G.; Gomez-Puertas, P.; Casals, N.
Molecular genetics of HMG-CoA lyase deficiency
Mol. Genet. Metab.
92
198-209
2007
Homo sapiens (P35914), Homo sapiens
Lin, W.D.; Wang, C.H.; Lai, C.C.; Tsai, Y.; Wu, J.Y.; Chen, C.P.; Tsai, F.J.
Molecular analysis of Taiwanese patients with 3-hydroxy-3-methylglutaryl CoA lyase deficiency
Clin. Chim. Acta
401
33-36
2009
Homo sapiens
Leung, A.A.; Chan, A.K.; Ezekowitz, J.A.; Leung, A.K.
A case of dilated cardiomyopathy associated with 3-hydroxy-3-methylglutaryl-coenzyme A (HMG CoA) lyase deficiency
Case Report Med.
2009
183125
2009
Homo sapiens
Reimao, S.; Morgado, C.; Almeida, I.T.; Silva, M.; Real, H.C.; Campos, J.
3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency: Initial presentation in a young adult
J. Inherit. Metab. Dis.
32
S49-52
2009
Homo sapiens
Montgomery, C.; Miziorko, H.M.
Influence of multiple cysteines on human 3-hydroxy-3-methylglutaryl-CoA lyase activity and formation of inter-subunit adducts
Arch. Biochem. Biophys.
511
48-55
2011
Homo sapiens (P35914), Homo sapiens
Fu, Z.; Runquist, J.A.; Montgomery, C.; Miziorko, H.M.; Kim, J.J.
Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes
J. Biol. Chem.
285
26341-26349
2010
Homo sapiens
Puisac, B.; Arnedo, M.; Casale, C.H.; Ribate, M.P.; Castiella, T.; Ramos, F.J.; Ribes, A.; Perez-Cerda, C.; Casals, N.; Hegardt, F.G.; Pie, J.
Differential HMG-CoA lyase expression in human tissues provides clues about 3-hydroxy-3-methylglutaric aciduria
J. Inherit. Metab. Dis.
33
405-410
2010
Homo sapiens
Nakagawa, S.; Kojima, Y.; Sekino, K.; Yamato, S.
Effect of polyphenols on 3-hydroxy-3-methylglutaryl-coenzyme A lyase activity in human hepatoma HepG2 cell extracts
Biol. Pharm. Bull.
36
1902-1906
2013
Homo sapiens
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