HOME
login
history
all enzymes
BRENDA home
History
Information on EC 4.2.1.18 - methylglutaconyl-CoA hydratase
for references in articles please use BRENDA:EC4.2.1.18Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.2.1.18 methylglutaconyl-CoA hydrataseSpecify your search results
Word Map
- 4.2.1.18
-
acidurias
-
3-methylglutaconic
- urine
- carboxylase
-
inborn
-
3-methylglutaric
- 3-methylcrotonyl-coa
-
speech
- acidosis
- enoyl-coas
-
rna-binding
-
hypotonia
-
3-hydroxyisovaleric
- isovaleryl-coa
- medicine
-
psychomotor
-
thiolase
The enzyme appears in viruses and cellular organisms
Synonyms
(3S)-methylglutaconyl-CoA hydratase, 3-methylglutaconyl CoA hydratase, 3-methylglutaconyl-CoA hydratase, 3-MG-CoA, 3-MGCoA-H, 3MGH, At4g16800, AU RNA binding protein/enoyl-Coenzyme A hydratase, AUH, HMG-CoA hydrolyase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(3S)-methylglutaconyl-CoA hydratase
3-methylglutaconyl CoA hydratase
3-methylglutaconyl-CoA hydratase
3-MGCoA-H
AU RNA binding protein/enoyl-Coenzyme A hydratase
-
enzyme also possesses an RNA-binding activity to AUUU repeats
AUH
HMG-CoA hydrolyase
-
-
-
-
hydratase, methylglutaconyl coenzyme A
-
-
-
-
LiuC
methylglutaconase
-
-
-
-
methylglutaconyl coenzyme A hydratase
-
-
-
-
MG-CoA hydratase
-
-
-
-
MGCH
Tb427.10.4000
3-methylglutaconyl CoA hydratase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H2O
-
-
-
-
(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H2O
syn-addition-elimination of H2O
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxy-3-methylglutaryl-CoA hydro-lyase (trans-3-methylglutaconyl-CoA-forming)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9024-24-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(R,S)-3-hydroxy-3-methylglutaryl-CoA
?
different co-substrates tested
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
isovalerate as sole carbon and energy source in Acinetobacter is metabolized via isovaleryl-CoA, oxidative (S)-leucine degradation pathway
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
isovalerate as sole carbon and energy source in Acinetobacter is metabolized via isovaleryl-CoA, oxidative (S)-leucine degradation pathway
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
-
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
-
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
catalyzes fifth step in the leucine degradation pathway
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
fifth step in the leucine degradation pathway
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
four types of the human disease 3-methylglutaconic aciduria distinguished, only form I is due to deficient activity of 3-methylglutaconyl-CoA hydratase leading to accumulation of 3-methylglutaconate
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
leucine degradation pathway, human AUH gene encoding a bifunctional enzyme with RNA-binding activity and enoyl-CoA-hydratase activity
-
-
?
trans-3-methylglutaconyl-CoA + H2O
(S)-3-hydroxymethylglutaryl-CoA
-
-
-
-
?
trans-3-methylglutaconyl-CoA + H2O
(S)-3-hydroxymethylglutaryl-CoA
-
-
-
-
?
additional information
?
-
-
no activity with crotonyl-CoA and methylcrotonyl-CoA
-
-
-
additional information
?
-
-
no activity with crotonyl-CoA and methylcrotonyl-CoA
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
trans-3-methylglutaconyl-CoA + H2O
isovalerate as sole carbon and energy source in Acinetobacter is metabolized via isovaleryl-CoA, oxidative (S)-leucine degradation pathway
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
isovalerate as sole carbon and energy source in Acinetobacter is metabolized via isovaleryl-CoA, oxidative (S)-leucine degradation pathway
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
-
catalyzes fifth step in the leucine degradation pathway
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
fifth step in the leucine degradation pathway
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
cofactors not identified in the purified enzyme fraction
-
additional information
cofactors not identified in the purified enzyme fraction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
stimulation by divalent metal ions such as Mg2+ not identified
additional information
stimulation by divalent metal ions such as Mg2+ not identified
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
acetyl-coa c-acetyltransferase deficiency
Screening for defects of branched-chain amino acid metabolism.
Acidosis, Lactic
Hypertrophic cardiomyopathy, cataract, developmental delay, lactic acidosis: a novel subtype of 3-methylglutaconic aciduria.
Barth Syndrome
Association of 3-methylglutaconic aciduria with sensori-neural deafness, encephalopathy, and Leigh-like syndrome (MEGDEL association) in four patients with a disorder of the oxidative phosphorylation.
Cardiomyopathy, Dilated
3-Methylglutaconyl-Coenzyme-A Hydratase Deficiency and the Development of Dilated Cardiomyopathy.
Cardiomyopathy, Hypertrophic
Hypertrophic cardiomyopathy, cataract, developmental delay, lactic acidosis: a novel subtype of 3-methylglutaconic aciduria.
Cataract
Hypertrophic cardiomyopathy, cataract, developmental delay, lactic acidosis: a novel subtype of 3-methylglutaconic aciduria.
Dehydration
Metabolic reconstructions identify plant 3-methylglutaconyl-CoA hydratase that is crucial for branched-chain amino acid catabolism in mitochondria.
Heart Failure
3-Methylglutaconyl-Coenzyme-A Hydratase Deficiency and the Development of Dilated Cardiomyopathy.
hydroxymethylglutaryl-coa lyase deficiency
3-Methylglutaconyl-CoA hydratase, 3-methylcrotonyl-CoA carboxylase and 3-hydroxy-3-methylglutaryl-CoA lyase deficiencies: a coupled enzyme assay useful for their detection.
hydroxymethylglutaryl-coa lyase deficiency
Screening for defects of branched-chain amino acid metabolism.
isovaleryl-coa dehydrogenase deficiency
Screening for defects of branched-chain amino acid metabolism.
Metabolic Diseases
3-Methylglutaconic aciduria type I: clinical heterogeneity as a neurometabolic disease.
methylcrotonoyl-coa carboxylase deficiency
Screening for defects of branched-chain amino acid metabolism.
methylglutaconyl-coa hydratase deficiency
3-Methylglutaconic aciduria type I: clinical heterogeneity as a neurometabolic disease.
methylglutaconyl-coa hydratase deficiency
3-Methylglutaconic aciduria-lessons from 50 genes and 977 patients.
methylglutaconyl-coa hydratase deficiency
3-Methylglutaconic and 3-methylglutaric aciduria in a patient with suspected 3-methylglutaconyl-CoA hydratase deficiency.
methylglutaconyl-coa hydratase deficiency
3-Methylglutaconyl-CoA hydratase deficiency: a new patient with speech retardation as the leading sign.
methylglutaconyl-coa hydratase deficiency
3-Methylglutaconyl-Coenzyme-A Hydratase Deficiency and the Development of Dilated Cardiomyopathy.
methylglutaconyl-coa hydratase deficiency
Leucine Loading Test is Only Discriminative for 3-Methylglutaconic Aciduria Due to AUH Defect.
methylglutaconyl-coa hydratase deficiency
Screening for defects of branched-chain amino acid metabolism.
Starvation
Metabolic reconstructions identify plant 3-methylglutaconyl-CoA hydratase that is crucial for branched-chain amino acid catabolism in mitochondria.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
addition of water to the (E)-isomer of 3-methylglutaconyl-CoA of the leucine degradative pathway, intermediate is (S)-3-hydroxy-3-methylglutaryl-CoA
-
additional information
additional information
addition of water to the (E)-isomer of 3-methylglutaconyl-CoA of the leucine degradative pathway, intermediate is (S)-3-hydroxy-3-methylglutaryl-CoA
-
additional information
additional information
-
kinetic constants determined by HPLC and mass spectrometry, assay conditions indicated
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
calculated with the subunit molecular mass of 3-methylglutaconyl-CoA hydratase of 28800 Dalton
-
additional information
additional information
calculated with the subunit molecular mass of 3-methylglutaconyl-CoA hydratase of 28800 Dalton
-
additional information
additional information
-
kinetic constants determined by HPLC and mass spectrometry
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
assay in presence of 0.5 ml 50 mM potassium phosphate pH 7.0 and 0.1 mM glutaconyl-CoA, kinetic constants determined by HPLC, 3-methylated CoA-thiol esters identified as the real substrates as expected from the pathway of isovalerate oxidation, specificity constants of other substrates as glutaconyl-CoA and 3-hydroxyglutaryl-CoA are 22 and 7 times lower, no activities measured for crotonyl-CoA
additional information
assay in presence of 0.5 ml 50 mM potassium phosphate pH 7.0 and 0.1 mM glutaconyl-CoA, kinetic constants determined by HPLC, 3-methylated CoA-thiol esters identified as the real substrates as expected from the pathway of isovalerate oxidation, specificity constants of other substrates as glutaconyl-CoA and 3-hydroxyglutaryl-CoA are 22 and 7 times lower, no activities measured for crotonyl-CoA
additional information
-
highly sensitive assay method, that allows reliable determination of enzyme activity in crude extract
additional information
-
direct nonisotopic activity assay in human skin fibroblast homogenates developed, products analyzed by HPLC, AUH-decifiency by mutations reveals 9% of the wild-type enzyme activity and increased levels of 3-methylglutaric acid and 3-hydroxyisovaleric acid
additional information
-
activity of 3-methylglutaconyl-CoA hydratase measured in fibroblasts within normal limits in all patients, urinary organic acid analysis determined by HPLC or mass spectrometry, increase of 3-methylglutaconic acid in all cases, and 3-methylglutaric acid in four out five patients, three novel subtypes of the diseease 3-methylglutaconic aciduria not coupled to impaired activity of 3-methylglutaconyl-CoA hydratase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
pH 6.0: about 80% of maximal activity, pH 8.5: about 50% of maximal activity
7 - 7.4
-
kinetic constants determined at pH 7.4, direct nonisotopic activity assay in human skin fibroblasts at pH 7.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSMZ 11652, strain IVS-B, formerly classified as Mycobacterium IVS-B
SwissProt
brenda
DSMZ 11652, strain IVS-B, formerly classified as Mycobacterium IVS-B
SwissProt
brenda
patients with methylglutaconyl-CoA hydratase deficiency with diverse clinical syndromes
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme is expressed in both insect and mammalian bloodstream forms of Trypanosoma brucei
brenda
-
enzyme is expressed in both insect and mammalian bloodstream forms of Trypanosoma brucei
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme deficiency, due to homozygous deletion of exons 1-3 within the AUH gene, leads to 3-methylglutaconic aciduria type I with phenotypic heterogeneity, e.g. learning disability, attention deficit-hyperactivity and early onset subclinical leukoencephalopathy or severe expressive speech delay and delay in speech sound development with normal cognitive functions, overview
physiological function
physiological function
-
the depletion of 3-MGCoA-H by RNAi affects minimally the proliferation of both insect and mammalian bloodstream forms. An excess of leucine in the culture medium causes growth defects in cells depleted of 3-MGCoA-H, which can be reestablished by mevalonate. Procyclics depleted of the 3-MGCoA-H present reduced levels of synthesized steroids relative to cholesterol that is scavenged by the parasite
physiological function
at4g16800 knockout plants subjected to dark-induced carbon starvation, display accelerated senescence in their rosette leaves as compared with control plants, and a marked increase in the accumulation of free and total leucine, isoleucine and valine. The seeds of the at4g16800 mutant show a similar accumulation of free branched-chain amino acids
physiological function
-
the depletion of 3-MGCoA-H by RNAi affects minimally the proliferation of both insect and mammalian bloodstream forms. An excess of leucine in the culture medium causes growth defects in cells depleted of 3-MGCoA-H, which can be reestablished by mevalonate. Procyclics depleted of the 3-MGCoA-H present reduced levels of synthesized steroids relative to cholesterol that is scavenged by the parasite
-
Show AA Sequence and Transmembrane Helices (376 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
221400
-
mass spectroscopy, in the presence of a long RNA containing 24 repeats of the AUUU motif, (AUUU)24A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer or trimer
-
AUH trimer dimerizes upon binding to one molecule of a long RNA containing 24 repeats of the AUUU motif, (AUUU)24A, determined by mass-spectroscopy
homotetramer
homotetramer
4 * 28800, four identical subunits, determined by SDS-PAGE
homotetramer
-
4 * 28800, four identical subunits, determined by SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AUH is crystallized with a long RNA containing 24 repeats of the AUUU motif. AUH structure is determined as an asymmetric dimer of trimers with a kink in the alignment of the trimer axes, resulting in the formation of two clefts with significantly different sizes
-
structures refined to 2.05 and 1.1 A, in the apo form and bound to coenzyme A, respectively. The dehydration of 3-hydroxy-3-methylglutaryl CoA to 3-methylglutaconyl CoA involves Glu112 and Glu132 and likely employs the typical crotonase acid-base mechanism. Residues Tyr231 and Arg69 are key players in positioning the substrate to enable catalysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E138D
-
the ratio of turnover number to KM-value is 9fold lower than the wild-type ratio
E138Q
-
the ratio of turnover number to KM-value is 3600fold lower than the wild-type ratio
G118E
-
no activity with crotonyl-CoA, methylcrotonyl-CoA and methylglutaconyl-CoA
E138D
-
the ratio of turnover number to KM-value is 9fold lower than the wild-type ratio
-
E138Q
-
the ratio of turnover number to KM-value is 3600fold lower than the wild-type ratio
-
G118E
-
no activity with crotonyl-CoA, methylcrotonyl-CoA and methylglutaconyl-CoA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from cell-free extracts of isovalerate-grown cells of Acinetobacter strain IVS-B by gel-filtration and SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, amino acid sequence determined, membership to the crotonase/isomerase super family classified by comparing protein seqences, up to 50% identity to amino acid sequences of more than 100 prokaryotic enoyl-CoA hydratases, 30% homology to the gene product of human AUH gene
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
sensitive and specific enzymatic assay for 3-methylglutaconyl-CoA hydratase that enables the rapid enzymatic diagnosis of 3-methylglutaconic aciduria type I in cultured skin fibroblasts without the need for radiochemicals
medicine
-
studies on the metabolic disease 3-methylglutaconic aciduria type I, characterized by abnormal organic acid profile and excessive urinary excretion of 3-methylglutaconic acid, 3-methylglutaric acid and 3-hydroxyisovaleric acid
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Ovis aries
-
brenda
Hilz, H.; Knappe, J.; Ringelmann, E.; Lynen, F.
Methylglutaconase, eine neue Hydratase, die am Stoffwechsel verzweigter Carbonsaeuren beteiligt ist
Biochem. Z.
329
476-489
1958
Bos taurus
-
brenda
Hermans-Lokkerbol, A.; van der Heijden, R.; Verpoorte, R.
Isocratic high-performance liquid chromatography of coenzyme A esters involved in the metabolism of 3S-hydroxy-3-methylglutaryl-coenzyme A. Detection of related enzyme activities in Catharanthus roseus plant cell culture
J. Chromatogr. A
752
123-130
1996
Catharanthus roseus
-
brenda
Gibson, K.M.
Assay of 3-methylglutaconyl-CoA hydratase
Methods Enzymol.
166
214-218
1988
Homo sapiens
brenda
Gibson, K.M.
3-Methylglutaconyl-coenzyme-A hydratase deficiency: a new case
J. Inherit. Metab. Dis.
15
363-366
1992
Homo sapiens
brenda
Narisawa, K.; Gibson, K.M.; Sweetman, L.; Nyhan, W.L.
3-Methylglutaconyl-CoA hydratase, 3-methylcrotonyl-CoA carboxylase and 3-hydroxy-3-methylglutaryl-CoA lyase deficiencies: a coupled enzyme assay useful for their detection
Clin. Chim. Acta
184
57-64
1989
Homo sapiens
brenda
Van der Heijden, R.; de Boer-Hlupa, V.; Verpoorte, R.; Duine, J.A.
Enzymes involved in the metabolism of 3-hydroxy-3-methylglutaryl-coenzyme A in Catharanthus roseus
Plant Cell
38
345-349
1994
Catharanthus roseus
-
brenda
Wong, B.J.; Gerlt, J.A.
Evolution of function in the crotonase superfamily: (3S)-methylglutaconyl-CoA hydratase from Pseudomonas putida
Biochemistry
43
4646-4654
2004
Pseudomonas putida, Pseudomonas putida PA2011
brenda
Loupatty, F.J.; Ruiter, J.P.N.; Ijlst, L.; Duran, M.; Wanders, R.J.A.
Direct nonisotopic assay of 3-methylglutaconyl-CoA hydratase in cultured human skin fibroblasts to specifically identify patients with 3-methylglutaconic aciduria type I
Clin. Chem.
50
1447-1450
2004
Homo sapiens
brenda
Mack, M.; Liesert, M.; Zschocke, J.; Peters, V.; Linder, D.; Buckel, W.
3-Methylglutaconyl-CoA hydratase from Acinetobacter sp
Arch. Microbiol.
185
297-306
2006
Acinetobacter sp., Acinetobacter sp. (Q3HW12), Acinetobacter sp. DSM 11652 (Q3HW12)
brenda
Mack, M.; Schniegler-Mattox, U.; Peters, V.; Hoffmann, G.F.; Liesert, M.; Buckel, W.; Zschocke, J.
Biochemical characterization of human 3-methylglutaconyl-CoA hydratase and its role in leucine metabolism
FEBS J.
273
2012-2022
2006
Homo sapiens, Homo sapiens (Q13825)
brenda
Di Rosa, G.; Deodato, F.; Loupatty, F.J.; Rizzo, C.; Carrozzo, R.; Santorelli, F.M.; Boenzi, S.; DAmico, A.; Tozzi, G.; Bertini, E.; Maiorana, A.; Wanders, R.J.; Dionisi-Vici, C.
Hypertrophic cardiomyopathy, cataract, developmental delay, lactic acidosis: a novel subtype of 3-methylglutaconic aciduria
J. Inherit. Metab. Dis.
29
546-550
2006
Homo sapiens, Homo sapiens (Q13825)
brenda
Kurimoto, K.; Kuwasako, K.; Sandercock, A.; Unzai, S.; Robinson, C.; Muto, Y.; Yokoyama, S.
AU-rich RNA-binding induces changes in the quaternary structure of AUH
Proteins
75
360-372
2009
Homo sapiens, Homo sapiens (Q13825)
brenda
Mercimek-Mahmutoglu, S.; Tucker, T.; Casey, B.
Phenotypic heterogeneity in two siblings with 3-methylglutaconic aciduria type I caused by a novel intragenic deletion
Mol. Genet. Metab.
104
410-413
2011
Homo sapiens
brenda
Su, B.; Ryan, R.O.
Metabolic biology of 3-methylglutaconic acid-uria: a new perspective
J. Inherit. Metab. Dis.
37
359-368
2014
Homo sapiens (Q13825)
brenda
Bock, T.; Reichelt, J.; Mueller, R.; Blankenfeldt, W.
The Structure of LiuC, a 3-hydroxy-3-methylglutaconyl CoA dehydratase involved in isovaleryl-CoA biosynthesis in Myxococcus xanthus, reveals insights into specificity and catalysis
ChemBioChem
17
1658-1664
2016
Myxococcus xanthus (Q1D5Y4), Myxococcus xanthus DK 1622 (Q1D5Y4)
brenda
de Lima Stein, M.L.; Icimoto, M.Y.; de Castro Levatti, E.V.; Oliveira, V.; Straus, A.H.; Schenkman, S.
Characterization and role of the 3-methylglutaconyl coenzyme A hidratase in Trypanosoma brucei
Mol. Biochem. Parasitol.
214
36-46
2017
Trypanosoma brucei, Trypanosoma brucei Lister 427
brenda
Latimer, S.; Li, Y.; Nguyen, T.T.H.; Soubeyrand, E.; Fatihi, A.; Elowsky, C.G.; Block, A.; Pichersky, E.; Basset, G.J.
Metabolic reconstructions identify plant 3-methylglutaconyl-CoA hydratase that is crucial for branched-chain amino acid catabolism in mitochondria
Plant J.
95
358-370
2018
Arabidopsis thaliana (F4JML5)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 4.2.1.18)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
