酵素系統名
WordNet
- any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions
PrepTutorEJDIC
- 酵素
- (各分野で用いる)専門用語法 / (体系に基づく)科学的命名法
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/06/08 21:33:20」(JST)
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Not to be confused with European Commission number.
The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze.[1]
As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
Strictly speaking, EC numbers do not specify enzymes, but enzyme-catalyzed reactions. If different enzymes (for instance from different organisms) catalyze the same reaction, then they receive the same EC number.[2] Furthermore, through convergent evolution, completely different protein folds can catalyze an identical reaction and therefore would be assigned an identical EC number (these are called non-homologous isofunctional enzymes, or NISE).[3] By contrast, UniProt identifiers uniquely specify a protein by its amino acid sequence.[4]
Contents
- 1 Format of number
- 2 Top level codes
- 3 Reaction Similarity
- 4 History
- 5 See also
- 6 References
- 7 External links
Format of number
Every enzyme code consists of the letters "EC" followed by four numbers separated by periods. Those numbers represent a progressively finer classification of the enzyme.
For example, the tripeptide aminopeptidases have the code "EC 3.4.11.4", whose components indicate the following groups of enzymes:
- EC 3 enzymes are hydrolases (enzymes that use water to break up some other molecule)
- EC 3.4 are hydrolases that act on peptide bonds
- EC 3.4.11 are those hydrolases that cleave off the amino-terminal amino acid from a polypeptide
- EC 3.4.11.4 are those that cleave off the amino-terminal end from a tripeptide
Top level codes
Top-level EC numbers[5]
| Group |
Reaction catalyzed |
Typical reaction |
Enzyme example(s) with trivial name |
EC 1
Oxidoreductases |
To catalyze oxidation/reduction reactions; transfer of H and O atoms or electrons from one substance to another |
AH + B → A + BH (reduced)
A + O → AO (oxidized) |
Dehydrogenase, oxidase |
EC 2
Transferases |
Transfer of a functional group from one substance to another. The group may be methyl-, acyl-, amino- or phosphate group |
AB + C → A + BC |
Transaminase, kinase |
EC 3
Hydrolases |
Formation of two products from a substrate by hydrolysis |
AB + H2O → AOH + BH |
Lipase, amylase, peptidase |
EC 4
Lyases |
Non-hydrolytic addition or removal of groups from substrates. C-C, C-N, C-O or C-S bonds may be cleaved |
RCOCOOH → RCOH + CO2 or [X-A-B-Y] → [A=B + X-Y] |
Decarboxylase |
EC 5
Isomerases |
Intramolecule rearrangement, i.e. isomerization changes within a single molecule |
AB → BA |
Isomerase, mutase |
EC 6
Ligases |
Join together two molecules by synthesis of new C-O, C-S, C-N or C-C bonds with simultaneous breakdown of ATP |
X + Y+ ATP → XY + ADP + Pi |
Synthetase |
Reaction Similarity
Similarity between enzymatic reactions (EC) can be calculated by using bond changes, reaction centres or substructure metrics (i.e. EC-BLAST).[6]
History
The enzyme nomenclature scheme was developed starting in 1955, when the International Congress of Biochemistry in Brussels set up an Enzyme Commission. The first version was published in 1961. The current sixth edition, published by the International Union of Biochemistry and Molecular Biology in 1992, contains 3196 different enzymes. Supplements 1-4 were published 1993-1999. Subsequent supplements have been published electronically, at the website of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.[5]
See also
- List of EC numbers
- List of enzymes
- TC number (classification of membrane transport proteins)
References
- ^ Webb EC (1992). Enzyme nomenclature 1992: recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the nomenclature and classification of enzymes. San Diego: Published for the International Union of Biochemistry and Molecular Biology by Academic Press. ISBN 0-12-227164-5.
- ^ "ENZYME (Enzyme nomenclature database)". ExPASy. Retrieved 2006-03-14.
- ^ Omelchenko MV, Galperin MY, Wolf YI, Koonin EV (2010). "Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution". Biol. Direct 5: 31. doi:10.1186/1745-6150-5-31. PMC 2876114. PMID 20433725.
- ^ Apweiler R, Bairoch A, Wu CH, Barker WC, Boeckmann B, Ferro S, Gasteiger E, Huang H, Lopez R, Magrane M, Martin MJ, Natale DA, O'Donovan C, Redaschi N, Yeh LS (January 2004). "UniProt: the Universal Protein knowledgebase". Nucleic Acids Res. 32 (Database issue): D115–9. doi:10.1093/nar/gkh131. PMC 308865. PMID 14681372.
- ^ a b Moss GP. "Recommendations of the Nomenclature Committee". International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes by the Reactions they Catalyse. Retrieved 2006-03-14.
- ^ Rahman, SA; Cuesta, SM; Furnham, N; Holliday, GL; Thornton, JM (2014). "EC-BLAST: a tool to automatically search and compare enzyme reactions". Nature Methods 11: 171–174. doi:10.1038/nmeth.2803. PMID 24412978.
External links
- Enzyme Nomenclature, authoritative website by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, maintained by G.P. Moss
- Enzyme nomenclature database — by ExPASy
- List of all EC numbers — by BRENDA
- Browse PDB structures by EC number
- Browse SCOP domains by EC number — by dcGO
- Compare EC numbers using EC-Blast
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Proteins: enzymes
|
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
| Classification |
- Enzyme superfamily
- EC number
- List of enzymes
|
|
| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
|
|
- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
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UpToDate Contents
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English Journal
- What's My Substrate? Computational Function Assignment of Candida parapsilosis ADH5 by Genome Database Search, Virtual Screening, and QM/MM Calculations.
- Dhoke GV1, Ensari Y1, Davari MD1, Ruff AJ1, Schwaneberg U1,2, Bocola M1.
- Journal of chemical information and modeling.J Chem Inf Model.2016 Jul 25;56(7):1313-23. doi: 10.1021/acs.jcim.6b00076. Epub 2016 Jul 15.
- Zinc-dependent medium chain reductase from Candida parapsilosis can be used in the reduction of carbonyl compounds to pharmacologically important chiral secondary alcohols. To date, the nomenclature of cpADH5 is differing (CPCR2/RCR/SADH) in the literature, and its natural substrate is not known. In
- PMID 27387009
- Xenobiotic/medium chain fatty acid: CoA ligase - a critical review on its role in fatty acid metabolism and the detoxification of benzoic acid and aspirin.
- van der Sluis R1, Erasmus E1.
- Expert opinion on drug metabolism & toxicology.Expert Opin Drug Metab Toxicol.2016 Jul 15:1-11. [Epub ahead of print]
- INTRODUCTION: Activation of fatty acids by the acyl-CoA synthetases (ACSs) is the vital first step in fatty acid metabolism. The enzymatic and physiological characterization of the human xenobiotic/medium chain fatty acid: CoA ligases (ACSMs) has been severely neglected even though xenobiotics, such
- PMID 27351777
- Cloning, molecular characterisation and phylogeny of two evolutionary distinct glutamine synthetase isoforms in the green microalga Haematococcus pluvialis (Chlorophyceae).
- Reinecke DL1, Zarka A2, Leu S2, Boussiba S2.
- Journal of phycology.J Phycol.2016 Jul 12. doi: 10.1111/jpy.12444. [Epub ahead of print]
- Haematococcus pluvialis (Chlorophyta) is a widely used microalga of great economic potential, yet its molecular genetics and evolution are largely unknown. We present new detailed molecular and phylogenetic analysis of two glutamine synthetase (GS) enzymes and genes (gln) under the Astaxanthin-induc
- PMID 27402429
Japanese Journal
- 1980-2009年の30年間における新有効成分含有医薬品（NAIs)<br/>—標的酵素の反応特性と NAIs 創出の推移—
- 血清および脳脊髄液中のN-methyl-D-aspartateレセプターサブユニットNR2に対する抗体の固相化酵素抗体法による測定 ―全身性エリテマトーデス患者について―
- 必須アミノ酸, 非必須アミノ酸 その二つを分けるもの
- 日本栄養・食糧学会誌 : Nippon eiy◆U014D◆ shokury◆U014D◆ gakkaishi = Journal of Japanese Society of Nutrition and Food Science 60(3), 137-149, 2007-06-10
- NAID 10026885614
Related Links
- In Enzyme Nomenclature 1992 there was a section on general principles; recommended and systematic names; scheme of classification and numbering of enzymes; and rules for classification and nomenclature. This web version ...
- ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB ...
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