This article is about the group of enzymes. For the language, see Lyase language.
In biochemistry, a lyase is an enzyme that catalyzes the breaking (an "elimination" reaction) of various chemical bonds by means other than hydrolysis (a "substitution" reaction) and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible (called a "Michael addition"). For example, an enzyme that catalyzed this reaction would be a lyase:
ATP → cAMP + PPi
Lyases differ from other enzymes in that they require only one substrate for the reaction in one direction, but two substrates for the reverse reaction.
Contents
1Nomenclature
2Classification
3Membrane-associated lyases
4See also
5References
Nomenclature
Systematic names are formed as "substrate group-lyase." Common names include decarboxylase, dehydratase, aldolase, etc. When the product is more important, synthase may be used in the name, e.g. phosphosulfolactate synthase (EC 4.4.1.19, Michael addition of sulfite to phosphoenolpyruvate). A combination of both an elimination and a Michael addition is seen in O-succinylhomoserine (thiol)-lyase (MetY or MetZ) which catalyses first the γ-elimination of O-succinylhomoserine (with succinate as a leaving group) and then the addition of sulfide to the vinyl intermediate, this reaction was first classified as a lyase (EC 4.2.99.9), but was then reclassified as a transferase (EC 2.5.1.48).
Classification
Lyases are classified as EC 4 in the EC number classification of enzymes. Lyases can be further classified into seven subclasses:
EC 4.1 includes lyases that cleave carbon-carbon bonds, such as decarboxylases (EC 4.1.1), aldehyde lyases (EC 4.1.2), oxo acid lyases (EC 4.1.3), and others (EC 4.1.99)
EC 4.2 includes lyases that cleave carbon-oxygen bonds, such as dehydratases
EC 4.3 includes lyases that cleave carbon-nitrogen bonds
EC 4.4 includes lyases that cleave carbon-sulfur bonds
EC 4.5 includes lyases that cleave carbon-halide bonds
EC 4.6 includes lyases that cleave phosphorus-oxygen bonds, such as adenylyl cyclase and guanylyl cyclase
EC 4.99 includes other lyases, such as ferrochelatase
Membrane-associated lyases
Some lyases associate with biological membranes as peripheral membrane proteins or anchored through a single transmembrane helix[1].
See also
List of EC numbers of enzymes belonging to category EC 4
References
^Superfamilies of single-pass transmembrane lyases in Membranome database
EC 4 Introduction from the Department of Chemistry at Queen Mary, University of London
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For other people named Noor Jahan, see Noor Jahan (disambiguation). Nur Jahan نور جہاں Padshah Begum Idealized portrait of the Mughal empress Nur Jahan Empress consort of the Mughal Empire Tenure 25 May 1611 - 28 October 1627 Coronation 1611 Predecessor Saliha Banu Begum Successor Mumtaz Mahal Naib-i-Sultanat of the Mughal Empire Tenure 1616 - 28 October 1627 Born Mehr-un-Nissa 31 May 1577 Kandahar, Afghanistan Died 17 December 1645 (1645-12-17) (aged 68) Lahore, Mughal Empire (present-day Pakistan) Burial Tomb of Nur Jahan, Lahore Spouse Sher Afgan Khan ( m. 1594–1607) Jahangir ( m. 1611–1627) Issue Ladli Begum House Timurid (by marriage) Father Mirza Ghiyas Beg Mother Asmat Begam Religion Shia Islam Nur Jahan (born Mehr-un-Nissa ) (31 May 1577 – 18 December 1645 [1] ) was the twentieth (and last) wife of the Mughal emperor Jahangir. Nur Jahan was born Mehr-un-Nissa, the daughter of a Grand Vizier (Minister) who served...
