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Information on EC 4.2.1.18 - methylglutaconyl-CoA hydratase and Organism(s) Homo sapiens and UniProt Accession Q13825

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.18 methylglutaconyl-CoA hydratase
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Homo sapiens
UNIPROT: Q13825 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-methylglutaconyl-coa hydratase, 3-mgcoa-h, at4g16800, 3-methylglutaconyl coa hydratase, 3-mg-coa, methylglutaconyl-coa hydratase, (3s)-methylglutaconyl-coa hydratase, au rna binding protein/enoyl-coenzyme a hydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-methylglutaconyl CoA hydratase
-
3-methylglutaconyl-CoA hydratase
-
AU RNA binding protein/enoyl-Coenzyme A hydratase
enzyme also possesses an RNA-binding activity to AUUU repeats
3-methylglutaconyl CoA hydratase
-
-
-
-
3-methylglutaconyl-CoA hydratase
-
-
3MGH
-
-
HMG-CoA hydrolyase
-
-
-
-
hydratase, methylglutaconyl coenzyme A
-
-
-
-
methylglutaconase
-
-
-
-
methylglutaconyl coenzyme A hydratase
-
-
-
-
MG-CoA hydratase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxy-3-methylglutaryl-CoA hydro-lyase (trans-3-methylglutaconyl-CoA-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-24-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E)-3-methylglutaconyl-1-CoA
?
show the reaction diagram
different co-substrates tested
-
-
?
(E)-glutaconyl-CoA
?
show the reaction diagram
different co-substrates tested
-
-
?
(R,S)-3-hydroxy-3-methylglutaryl-CoA
?
show the reaction diagram
different co-substrates tested
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
show the reaction diagram
3-hydroxybutyryl-CoA
?
show the reaction diagram
different co-substrates tested
-
-
?
3-methylcrotonyl-CoA
?
show the reaction diagram
different co-substrates tested
-
-
?
crotonyl-CoA
?
show the reaction diagram
different co-substrates tested
-
-
?
trans-3-methylglutaconyl-CoA + H2O
(S)-3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
show the reaction diagram
-
penultimate step in Leu catabolism
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
show the reaction diagram
trans-3-methylglutaconyl-CoA + H2O
(S)-3-hydroxymethylglutaryl-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
(S)-3-hydroxy-3-methylglutaryl-CoA
trans-3-methylglutaconyl-CoA + H2O
show the reaction diagram
trans-3-methylglutaconyl-CoA + H2O
(S)-3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
-
-
-
?
(S)-3-Hydroxy-3-methylglutaryl-CoA
?
show the reaction diagram
-
penultimate step in Leu catabolism
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
(E)-3-methylglutaconyl-CoA
-
0.0024
(E)-glutaconyl-CoA
-
2.25
(R,S)-3-hydroxy-3-methylglutaryl-CoA
-
55.2
3-hydroxybutyryl-CoA
-
0.347
3-methylcrotonyl-CoA
-
12.1
crotonyl-CoA
-
0.0069 - 0.0094
(S)-3-hydroxymethylglutaryl-CoA
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.1
(E)-3-methylglutaconyl-CoA
-
1.4
(E)-glutaconyl-CoA
-
0.26
(R,S)-3-hydroxy-3-methylglutaryl-CoA
-
1.7
3-hydroxybutyryl-CoA
-
2.9
3-methylcrotonyl-CoA
-
6.8
crotonyl-CoA
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.4
kinetic constants determined at pH 7.4, direct nonisotopic activity assay in human skin fibroblasts at pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
activity assay in human skin fibroblasts at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cultured
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AUHM_HUMAN
339
0
35609
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
221400
mass spectroscopy, in the presence of a long RNA containing 24 repeats of the AUUU motif, (AUUU)24A
89980
mass spectroscopy, RNA free AUH
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
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
trimer
mainly exists as a trimer in solution, determined by mass-spectroscopy
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A240V
site-directed mutagenesis, nucleotide exchange C719T
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel-filtration and SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli using the pMAL-c2 expression vector
gene AUH, genotyping
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gibson, K.M.
Assay of 3-methylglutaconyl-CoA hydratase
Methods Enzymol.
166
214-218
1988
Homo sapiens
Manually annotated by BRENDA team
Gibson, K.M.
3-Methylglutaconyl-coenzyme-A hydratase deficiency: a new case
J. Inherit. Metab. Dis.
15
363-366
1992
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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 (Q13825), Homo sapiens
Manually annotated by BRENDA team
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 (Q13825), Homo sapiens
Manually annotated by BRENDA team
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 (Q13825), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team