メチルマロニルCoA脱炭酸酵素、メチルマロニルCoAデカルボキシラーゼ
- 関
- propionyl-CoA carboxylase
WordNet
- the 3rd letter of the Roman alphabet (同)c
- (music) the keynote of the scale of C major
- a general-purpose programing language closely associated with the UNIX operating system
- any of the enzymes that hydrolize the carboxyl group
PrepTutorEJDIC
- carbonの化学記号
- cobaltの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/09/25 17:18:09」(JST)
[Wiki en表示]
methylmalonyl-CoA decarboxylase |
Methylmalonyl CoA decarboxylase trimer, E.Coli
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Identifiers |
EC number |
4.1.1.41 |
CAS number |
37289-44-4 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / QuickGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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In enzymology, a methylmalonyl-CoA decarboxylase (EC 4.1.1.41) is an enzyme that catalyzes the chemical reaction
- (S)-methylmalonyl-CoA propanoyl-CoA + CO2
Hence, this enzyme has one substrate, (S)-methylmalonyl-CoA, and two products, propanoyl-CoA and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming). Other names in common use include propionyl-CoA carboxylase, propionyl coenzyme A carboxylase, methylmalonyl-coenzyme A decarboxylase, (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect], and (S)-methylmalonyl-CoA carboxy-lyase. This enzyme participates in propanoate metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EF8 and 1EF9.
References
- Galivan JH, Allen SH (1968). "Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus". J. Biol. Chem. 243 (6): 1253–61. PMID 5646172.
- Hilpert W, Dimroth P (1982). "Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient". Nature. 296 (5857): 584–5. PMID 7070502. doi:10.1038/296584a0.
- Hoffmann A, Hilpert W, Dimroth P (1989). "The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens". Eur. J. Biochem. 179 (3): 645–50. PMID 2920730. doi:10.1111/j.1432-1033.1989.tb14596.x.
Carbon-carbon lyases (EC 4.1)
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4.1.1: Carboxy-lyases |
- Acetoacetate decarboxylase
- Adenosylmethionine decarboxylase
- Arginine decarboxylase
- Aromatic L-amino acid decarboxylase
- Glutamate decarboxylase
- Histidine decarboxylase
- Lysine decarboxylase
- Malonyl-CoA decarboxylase
- Ornithine decarboxylase
- Oxaloacetate decarboxylase
- Phosphoenolpyruvate carboxykinase
- Phosphoenolpyruvate carboxylase
- Phosphoribosylaminoimidazole carboxylase
- Pyrophosphomevalonate decarboxylase
- Pyruvate decarboxylase
- RuBisCO
- Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase
- Uroporphyrinogen III decarboxylase
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4.1.2: Aldehyde-lyases |
- Fructose-bisphosphate aldolase
- Aldolase A
- Aldolase B
- Aldolase C
- 2-hydroxyphytanoyl-CoA lyase
- Threonine aldolase
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4.1.3: Oxo-acid-lyases |
- Isocitrate lyase
- 3-hydroxy-3-methylglutaryl-CoA lyase
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4.1.99: Other |
- Tryptophanase
- Photolyase
- CPD lyase
- Spore photoproduct lyase
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Enzymes
|
Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
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Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
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UpToDate Contents
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English Journal
- Phylogenetic distribution of three pathways for propionate production within the human gut microbiota.
- Reichardt N1, Duncan SH2, Young P2, Belenguer A2, McWilliam Leitch C2, Scott KP2, Flint HJ2, Louis P2.
- The ISME journal.ISME J.2014 Jun;8(6):1323-35. doi: 10.1038/ismej.2014.14. Epub 2014 Feb 20.
- Propionate is produced in the human large intestine by microbial fermentation and may help maintain human health. We have examined the distribution of three different pathways used by bacteria for propionate formation using genomic and metagenomic analysis of the human gut microbiota and by designin
- PMID 24553467
- Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity.
- Lietzan AD1, St Maurice M2.
- Archives of biochemistry and biophysics.Arch Biochem Biophys.2014 Feb 15;544:75-86. doi: 10.1016/j.abb.2013.10.014. Epub 2013 Oct 30.
- Biotin-dependent enzymes catalyze carboxylation, decarboxylation and transcarboxylation reactions that participate in the primary metabolism of a wide range of organisms. In all cases, the overall reaction proceeds via two half reactions that take place in physically distinct active sites. In the fi
- PMID 24184447
- Use of carglumic acid in the treatment of hyperammonaemia during metabolic decompensation of patients with propionic acidaemia.
- Abacan M1, Boneh A.
- Molecular genetics and metabolism.Mol Genet Metab.2013 Aug;109(4):397-401. doi: 10.1016/j.ymgme.2013.05.018. Epub 2013 Jun 6.
- Propionic acidaemia (PA) results from propionyl-CoA carboxylase deficiency. During metabolic decompensation, the accumulation of propionyl-CoA causes secondary hyperammonaemia through N-acetylglutamate synthetase inactivation. Carglumic acid, a structural analogue of N-acetylglutamate, was given to
- PMID 23791308
Japanese Journal
- Structural analysis of gene cluster encoding acetyl-CoA carboxylase from a deep-sea piezo- and psychrophilic bacterium, Shewanella violacea strain DSS 12
- 仲宗根 薫 [他]
- 近畿大学工学部研究報告 39, 15-18, 2005-12-20
- … Acetyl-CoA carboxylase is key enzyme involved in the starting for fatty acid synthesis. … In this study, we have cloned and sequenced gene cluster encoding acetyl-CoA carboxylase from a deep-sea piezo-and psychrophilic bacterium, Shewanella violacea strain DSS12. … The protein (AccA) encoded by the accA gene was strikingly similar to biotin carboxylase subunits of acetyl-CoA and propionyl-CoA carboxylases and of pyruvate carboxylase. …
- NAID 110005000932
- Methylmalonyl-CoA decarboxylaseの部分精製と酵素的性質, Galivan, J.H., Allen, S.H.G., Arch.Biochem.Biophys., 126,838,1968
Related Links
- Methylmalonyl-Coa Decarboxylase; Propionyl-CoA Carboxylase. On-line free medical diagnosis assistant. Ranked list of possible diseases from either several symptoms or a full patient history. A similarity measure between ... ...
- Species, Scientific Experts, Genomes and Genes, Research Grants, Publications, Research Topics about methylmalonyl coa decarboxylase ... ..The methylmalonyl-CoA rescued the dcm-1 mutant fruiting body and spore ...
★リンクテーブル★
[★]
- 英
- methylmalonyl-CoA decarboxylase
- 関
- メチルマロニルCoAデカルボキシラーゼ、プロピオニルCoAカルボキシラーゼ
[★]
- 英
- methylmalonyl-CoA decarboxylase
- 関
- メチルマロニルCoA脱炭酸酵素
[★]
[★]
[★]
デカルボキシラーゼ、脱炭酸酵素
- 関
- carboxy-lyase
[★]
補酵素A coenzyme A CoA
[★]
コバルト cobalt