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m First sentence indicated prosthetic groups are covalently linked to the apoprotein, but this is not necessarily so; changed it to say "tightly".
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{{Short description|Covalently bonded non-protein part of an enzyme}}
A '''prosthetic group''' is the non-amino acid component that is part of the structure of the heteroproteins or [[Conjugated protein|conjugated proteins]], being tightly linked to the [[Apoenzyme|apoprotein]].
 
Not to be confused with the [[Cofactor (biochemistry)|cofactorcosubstrate]] that binds to the [[enzyme]] apoenzyme (either a [[holoprotein]] or heteroprotein) by non-covalent binding a non-protein (non-[[amino acid]])
 
This is a component of a [[conjugated protein]] that is required for the protein's biological activity.<ref>{{cite web |url=http://www.chem.qmul.ac.uk/iupac/bioinorg/PR.html#24 |title=Glossary of Terms Used in Bioinorganic Chemistry: Prosthetic groups |accessdate=2007-10-30 |last=de Bolster |first=M.W.G. |date=1997 |publisher=International Union of Pure and Applied Chemistry |archive-url=https://wwwweb.webcitationarchive.org/6HWn4s3aU?url=web/20121128194239/http://www.chem.qmul.ac.uk/iupac/bioinorg/PR.html#24 |archive-date=20132012-0611-2028 |url-status=dead }}</ref> The prosthetic group may be [[organic compound|organic]] (such as a [[vitamin]], [[sugar]], [[RNA]], [[phosphate]] or [[lipid]]) or [[inorganic]] (such as a [[metal]] ion). Prosthetic groups are bound tightly to proteins and may even be attached through a [[covalent bond]]. They often play an important role in [[enzyme catalysis]]. A protein without its prosthetic group is called an [[Apoenzyme|apoprotein]], while a protein combined with its prosthetic group is called a [[holoprotein]]. A non-covalently bound prosthetic group cannot generally be removed from the holoprotein without denaturating the protein. Thus, the term "prosthetic group" is a very general one and its main emphasis is on the tight character of its binding to the apoprotein. It defines a ''structural'' property, in contrast to the term "coenzyme" that defines a ''functional'' property.
 
Prosthetic groups are a subset of [[Cofactor (biochemistry)|cofactors]]. Loosely bound metal ions and coenzymes are still cofactors, but are generally not called prosthetic groups.<ref>Metzler DE (2001) Biochemistry. The chemical reactions of living cells, 2nd edition, Harcourt, San Diego.</ref><ref>Nelson DL and Cox M.M (2000) Lehninger, Principles of Biochemistry, 3rd edition, Worth Publishers, New York </ref><ref>Campbell MK and Farrell SO (2009) Biochemistry, 6th edition, Thomson Brooks/Cole, Belmont, California</ref> In enzymes, prosthetic groups are involved in the catalytic mechanism and required for activity. Other prosthetic groups have structural properties. This is the case for the sugar and lipid moieties in [[glycoproteins]] and [[lipoproteins]] or [[RNA]] in ribosomes. They can be very large, representing the major part of the protein in [[proteoglycans]] for instance.
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== List of prosthetic groups ==
The table below contains a list of some of the most common prosthetic groups.
{| class="wikitable"
| '''Prosthetic group''' || '''Function''' || '''Distribution'''
|-
| [[Flavin mononucleotide]]&nbsp;<ref name="Joosten">{{cite journal |author=Joosten V, van Berkel WJ |title=Flavoenzymes |journal=Curr Opin Chem Biol |volume=11 |issue=2 |pages=195–202 |year=2007 |pmid=17275397 |doi=10.1016/j.cbpa.2007.01.010}}</ref> || [[Redox]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
| [[FAD|Flavin adenine dinucleotide]]&nbsp;<ref name="Joosten" /> || [[Redox]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
|[[Pyrroloquinoline quinone]]&nbsp;<ref>{{cite journal | author = Salisbury SA, Forrest HS, Cruse WB, Kennard O | title = A novel coenzyme from bacterial primary alcohol dehydrogenases | journal = Nature | year = 1979 | volume = 280 | issue = 5725 | pages = 843–4 | doi = 10.1038/280843a0| pmid = 471057 | bibcode = 1979Natur.280..843S | s2cid = 3094647 }} {{PMID|471057}}</ref> || [[Redox]] reactions || [[Bacteria]]
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|[[Biotin]]&nbsp;<ref>{{cite journal |author=Jitrapakdee S, Wallace JC |title=The biotin enzyme family: conserved structural motifs and domain rearrangements |journal=Curr. Protein Pept. Sci. |volume=4 |issue=3 |pages=217–29 |year=2003 |pmid=12769720 |doi=10.2174/1389203033487199}}</ref> || [[Carboxylation]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
| [[Methylcobalamin]]&nbsp;<ref>{{cite journal |author=Banerjee R, Ragsdale SW |title=The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes |journal=Annu. Rev. Biochem. |volume=72 |pages=209–47 |year=2003 |pmid=14527323 |doi=10.1146/annurev.biochem.72.121801.161828|s2cid=37393683 |url=https://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1458&context=biochemfacpub }}</ref> || [[Methylation]] and [[isomerisation]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
|[[Thiamine pyrophosphate]]&nbsp;<ref>{{cite journal |author=Frank RA, Leeper FJ, Luisi BF |title=Structure, mechanism and catalytic duality of thiamine-dependent enzymes |journal=Cell. Mol. Life Sci. |volume=64 |issue=7–8 |pages=892–905 |year=2007 |pmid=17429582 |doi=10.1007/s00018-007-6423-5|s2cid=20415735 |pmc=11136255 }}</ref> || Transfer of 2-carbon groups, α cleavage || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
|[[Heme]]&nbsp;<ref>{{cite journal |author=Wijayanti N, Katz N, Immenschuh S |title=Biology of heme in health and disease |journal=Curr. Med. Chem. |volume=11 |issue=8 |pages=981–6 |year=2004 |pmid=15078160 |doi=10.2174/0929867043455521}}</ref> || [[Oxygen]] binding and [[redox]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
|[[Molybdopterin]]&nbsp;<ref>{{cite journal |author=Mendel RR, Hänsch R |title=Molybdoenzymes and molybdenum cofactor in plants |journal=J. Exp. Bot. |volume=53 |issue=375 |pages=1689–98 |year=2002 |pmid=12147719 |doi=10.1093/jxb/erf038|doi-access=free }}</ref><ref>{{cite journal |author=Mendel RR, Bittner F |title=Cell biology of molybdenum |journal=Biochim. Biophys. Acta |volume=1763 |issue=7 |pages=621–35 |year=2006 |pmid=16784786 |doi=10.1016/j.bbamcr.2006.03.013|doi-access=free }}</ref> || [[Oxygenase|Oxygenation]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
|[[Lipoic acid]]&nbsp;<ref>{{cite journal |author=Bustamante J, Lodge JK, Marcocci L, Tritschler HJ, Packer L, Rihn BH |title=Alpha-lipoic acid in liver metabolism and disease |journal=Free Radic. Biol. Med. |volume=24 |issue=6 |pages=1023–39 |year=1998 |pmid=9607614 |doi=10.1016/S0891-5849(97)00371-7}}</ref> || [[Redox]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
|[[Cofactor F430]]
|[[Methanogenesis]]
|[[Archaea]]
|}
 
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