Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
3-hydroxy-3-methylglutaryl-CoA
acetoacetate + acetyl-CoA
Acetyl-CoA
?
-
enolization
-
-
?
additional information
?
-
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
-
leucine catabolism
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
-
involved in ketogenesis, leucine catabolism
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
-
involved in ketogenesis, leucine catabolism
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
-
involved in regulation of isoprenoid pathway
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
-
involved in ketogenesis, leucine catabolism
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
-
acetoacetate as fuel for extrahepatic tissues, involved in mevalonate synthesis
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
mechanism
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
stereochemistry
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
ir
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
Acetyl-CoA + acetoacetate
-
stereochemistry
-
-
?
3-hydroxy-3-methylglutaryl-CoA
acetoacetate + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA
acetoacetate + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA
acetoacetate + acetyl-CoA
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA
acetoacetate + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA
acetoacetate + acetyl-CoA
-
-
-
-
?
additional information
?
-
-
last step in ketogenesis
-
?
additional information
?
-
-
last step in ketogenesis
-
?
additional information
?
-
-
last step in ketogenesis
-
?
additional information
?
-
-
last step in ketogenesis
-
?
additional information
?
-
-
last step in ketogenesis
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0018 - 0.11
-
C237 mutants
0.03
recombinant deletion mutant Mut15, at 37°C
0.123
C170S/C266S mutant protein, pH not specified in the publication, temperature not specified in the publication
0.22
recombinant deletion mutant Mut12, at 37°C
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
1.13
recombinant deletion mutant Mut3, at 37°C
1.2
recombinant deletion mutant Mut6, at 37°C
1.27
recombinant deletion mutant Mut9, at 37°C
1.29
recombinant wild type enzyme, at 37°C
100.3
-
K48Q mutant protein, pH not specified in the publication, 30°C
117
-
HMGCLL1 mutant G2A, pH 8.2, 37°C
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
136
-
wild type protein, pH not specified in the publication, 30°C
150
-
wild-type HMGCLL1, pH 8.2, 37°C
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
249
-
mitochondrial enzyme
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
87.8
-
K48N mutant protein, pH not specified in the publication, 30°C
9.5
wild type enzyme, at 37°C
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
159
-
wild-type
159
-
wild-type HMGCL, pH 8.2, 37°C
348
-
C323S mutant
348
-
HMGCL mutant C323A, pH 8.2, 37°C
additional information
-
activities per g freshweight in mitochondrial and cytosolic fractions
additional information
-
-
additional information
-
organ-specific activities per unit freshweight
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
additional information
-
activities per g freshweight in mitochondrial and cytosolic fractions
additional information
-
tissue distribution of activities
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
A252A
decreased Km relative to the wild type enzyme
C238A
increased Km relative to the wild type enzyme
C238S
decreased Km relative to the wild type enzyme
D14E
decreased Km relative to the wild type enzyme
D176A
increased Km relative to the wild type enzyme
E44A
increased Km relative to the wild type enzyme
E9D
decreased Km relative to the wild type enzyme
H205A
increased Km relative to the wild type enzyme
H205D
increased Km relative to the wild type enzyme
H205R
decreased Km relative to the wild type enzyme
R13Q
increased Km relative to the wild type enzyme
V251A
decreased Km relative to the wild type enzyme
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)
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
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
K48Q
-
mimics Lys acetylation
L263P
lack of enzymatic activity
V70L
lack of enzymatic activity
C323S
-
shows less dithiothreitol activation than wild-type enzyme
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
-
decreased activity
D204N
-
reduced catalytic efficiency, mutation causes 3-hydroxy-3-methylgluratic aciduria in vivo
D204N
lack of enzymatic activity
D42A
-
4fold decrease in proton exchange
D42A
-
exhibits catalytic rates diminished by 130000fold
D42H
-
decreased activity
D42H
lack of enzymatic activity
E279K
lack of enzymatic activity
E279K
-
unstable recombinant protein
G203E
lack of enzymatic activity
G203E
the mutation causes 3-hydroxy-3-methylglutaric aciduria, it has less than 0.02% of the wild type enzyme activity
H233A
-
10fold decrease in proton exchange
H233A
-
exhibits catalytic rates diminished by 6400fold
H233R
-
decreased activity
H233R
lack of enzymatic activity
K48N
lack of enzymatic activity
K48N
the mutation causes 3-hydroxy-3-methylglutaric aciduria, shows less than 2% of wild type HMG-CoA lyase activity
K48N
-
inherited mutation
R41M
-
lower activity than R41Q mutant
R41M
-
catalytically deficient
R41Q
-
decreased activity
R41Q
-
mutation leads to human HMG-CoA lyase deficiency
R41Q
lack of enzymatic activity
R41Q
-
missense mutation causing 3-hydroxy-3-methylglutaric aciduria
S201Y
-
no activity
S201Y
-
no catalytic efficiency, mutation causes 3-hydroxy-3-methylgluratic aciduria in vivo
S201Y
lack of enzymatic activity
S75R
-
no activity
S75R
-
no catalytic efficiency, mutation causes 3-hydroxy-3-methylgluratic aciduria in vivo
S75R
lack of enzymatic activity
additional information
-
screening for enzyme mutants, identification of naturally occuring mutant FE6-C3 with disrupted gene encoding the enzyme
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
additional information
-
IVS3+1G to A, slice site mutation
additional information
-
IVS6-1G to A slice site mutation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Aragon, J.J.; Lowenstein, J.M.
A survey of enzymes which generate or use acetoacetyl thioesters in rat liver
J. Biol. Chem.
258
4725-4733
1983
Rattus norvegicus
brenda
Kramer, P.R.; Miziorko, H.M.
3-Hydroxy-3-methylglutaryl-CoA lyase: catalysis of acetyl coenzyme A enolization
Biochemistry
22
2353-2357
1983
Anas sp.
brenda
Kramer, P.R.; Miziorko, H.M.
Purification and characterization of avian liver 3-hydroxy-3-methylglutaryl coenzyme A lyase
J. Biol. Chem.
255
11023-11028
1980
Anas sp.
brenda
Zammit, V.A.
Localization of 3-hydroxy-3-methylglutaryl-CoA lyase and 3-oxo acid CoA-transferase in liver of three species of ruminants
Biochem. Soc. Trans.
8
543-544
1980
Capra hircus, Ovis aries
brenda
Clinkenbeard, K.D.; Reed, W.D.; Mooney, R.A.; Lane, M.D.
Intracellular localization of the 3-hydroxy-3-methylglutaryl coenzyme a cycle enzymes in liver
J. Biol. Chem.
250
3108-3116
1975
Gallus gallus, Rattus norvegicus
brenda
Messner, B.; Eggerer, H.; Cornforth, J.W.; Mallaby, R.
Substrate stereochemistry of the hydroxymethylglutaryl-CoA lyase and methylglutaconyl-CoA hydratase reactions
Eur. J. Biochem.
53
255-264
1975
Bos taurus
-
brenda
Narasimhan, C.; Roberts, J.R.; Miziorko, H.M.
Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl-CoA lyase: testing the function of the active site cysteine by site-directed mutation
Biochemistry
34
9930-9935
1995
Pseudomonas mevalonii
brenda
Bachhawat, B.K.; Robinson, W.G.; Coon, M.J.
The enzymatic cleavage of beta-hydroxy-beta-methylglutaryl coenzyme A to acetoacetate and acetyl coenzyme A
J. Biol. Chem.
216
727-736
1955
Columba livia, Sus scrofa
brenda
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
brenda
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
brenda
Hruz, P.W.; Miziorko, H.M.
Avian 3-hydroxy-3-methylglutaryl-CoA lyase: sensitivity of enzyme activity to thiol/disulfide exchange and identification of proximal reactive cysteines
Protein Sci.
1
1144-1153
1992
Gallus gallus, Tetrahymena pyriformis
brenda
Weber, T.; Bach, T.J.
Partial purification and characterization of membrane-associated 3-hydroxy-3-methylglutaryl coenzyme A lyase from radish seedlings
Z. Naturforsch. C
48
444-450
1993
Raphanus sativus
-
brenda
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
brenda
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
brenda
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
brenda
Narasimhan, C.; Miziorko, H.M.
Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl-CoA lyase: characterization of the isolated recombinant protein and investigation of the enzyme's cation requirements
Biochemistry
31
11224-11230
1992
Pseudomonas mevalonii
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Miziorko, H.M.; Narasimhan, C.
Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl-CoA lyase
Methods Enzymol.
324
139-149
2000
Pseudomonas mevalonii
brenda
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
brenda
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
brenda
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 (O34873), Bacillus subtilis, Brucella melitensis (Q8YEF2), Brucella melitensis
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
Leipnitz, G.; Seminotti, B.; Haubrich, J.; Dalcin, M.B.; Dalcin, K.B.; Solano, A.; de Bortoli, G.; Rosa, R.B.; Amaral, A.U.; Dutra-Filho, C.S.; Latini, A.; Wajner, M.
Evidence that 3-hydroxy-3-methylglutaric acid promotes lipid and protein oxidative damage and reduces the nonenzymatic antioxidant defenses in rat cerebral cortex
J. Neurosci. Res.
86
683-693
2008
Rattus norvegicus (P97519)
brenda
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
brenda
Leipnitz, G.; Seminotti, B.; Fernandes, C.G.; Amaral, A.U.; Beskow, A.P.; da Silva, L.d.e..B.; Zanatta, A.; Ribeiro, C.A.; Vargas, C.R.; Wajner, M.
Striatum is more vulnerable to oxidative damage induced by the metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency as compared to liver
Int. J. Dev. Neurosci.
27
351-356
2009
Rattus norvegicus
brenda
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
brenda
Chavez-Aviles, M.; Diaz-Perez, A.L.; Campos-Garcia, J.
The bifunctional role of LiuE from Pseudomonas aeruginosa, displays additionally HIHG-CoA lyase enzymatic activity
Mol. Biol. Rep.
37
1787-1791
2010
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO1SM
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Isaac, D.T.; Coady, A.; Van Prooyen, N.; Sil, A.
The 3-hydroxy-methylglutaryl coenzyme A lyase HCL1 is required for macrophage colonization by human fungal pathogen Histoplasma capsulatum
Infect. Immun.
81
411-420
2013
Histoplasma capsulatum
brenda
Montgomery, C.; Pei, Z.; Watkins, P.A.; Miziorko, H.M.
Identification and characterization of an extramitochondrial human 3-hydroxy-3-methylglutaryl-CoA lyase
J. Biol. Chem.
287
33227-33236
2012
Homo sapiens
brenda
Dong, Y.; Zhang, J.; Xu, R.; Lv, X.; Wang, L.; Sun, A.; Wei, D.
Insertion mutation in HMG-CoA lyase increases the production yield of MPA through Agrobacterium tumefaciens-mediated transformation
J. Microbiol. Biotechnol.
26
1924-1932
2016
Penicillium brevicompactum, Penicillium brevicompactum ATCC 16024
brenda