Editing Peripheral membrane protein (section)

===Enzymes===
Peripheral enzymes participate in [[metabolism]] of different membrane components, such as lipids ([[phospholipase]]s and [[cholesterol oxidase]]s), [[cell wall]] [[oligosaccharides]] ([[glycosyltransferase]] and [[transglycosidases]]), or proteins ([[signal peptidase]] and [[palmitoyl protein thioesterase]]s). [[Lipases]] can also digest lipids that form [[micelle]]s or nonpolar droplets in water.

{| class="wikitable" style="margin: 1em auto 1em auto"
!width="180"|Class
!width="275"|Function
!width="305"| Physiology
!width="50"| Structure
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| [[Alpha/beta hydrolase fold]] || Catalyzes the [[hydrolysis]] of chemical bonds.<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00561 |title=Pfam entry Abhydrolase 1 |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929115310/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00561 |archive-date=2007-09-29 |url-status=dead }}</ref>|| Includes [[bacteria]]l, [[fungal]], gastric and pancreatic [[lipase]]s, palmitoyl protein [[thioesterase]]s, [[cutin]]ase, and [[cholinesterase]]s ||central beta sheet inserted in between two layers of alpha helices<ref>{{Cite journal |last1=Bauer |first1=Tabea L. |last2=Buchholz |first2=Patrick C. F. |last3=Pleiss |first3=Jürgen |date=March 2020 |title=The modular structure of α/β-hydrolases |journal=The FEBS Journal |language=en |volume=287 |issue=5 |pages=1035–1053 |doi=10.1111/febs.15071 |issn=1742-464X|doi-access=free |pmid=31545554 }}</ref>
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| [[Phospholipase A2]] (secretory and cytosolic) || Hydrolysis of sn-2 [[fatty acid]] bond of [[phospholipid]]s.<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00068 |title=Pfam entry: Phospholipase A2 |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929110908/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00068 |archive-date=2007-09-29 |url-status=dead }}</ref>||Lipid digestion, membrane disruption, and [[lipid signaling]]. ||contains catalytic amino acid triad: [[aspartic acid]], [[serine]], and [[histidine]]<ref>{{Citation |last1=Casale |first1=Jarett |title=Biochemistry, Phospholipase A2 |date=2023 |url=http://www.ncbi.nlm.nih.gov/books/NBK534851/ |work=StatPearls |access-date=2023-11-29 |place=Treasure Island (FL) |publisher=StatPearls Publishing |pmid=30521272 |last2=Kacimi |first2=Salah Eddine O. |last3=Varacallo |first3=Matthew}}</ref> 
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| [[Phospholipase C]] || Hydrolyzes PIP2, a [[phosphatidylinositol]], into two second messagers, [[inositol triphosphate]] and [[diglyceride|diacylglycerol]].<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00388 |title=Pfam entry: Phosphatidylinositol-specific phospholipase C, X domain |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929084148/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00388 |archive-date=2007-09-29 |url-status=dead }}</ref> || [[Lipid signaling]] ||core structure composed of a split [[triosephosphate isomerase]] (TIM) barrel which has an active site, catalytic residues, and a Ca<sup>2+</sup> binding site <ref>{{Citation |title=Phospholipase C |date=2023-08-16 |url=https://en.wikipedia.org/w/index.php?title=Phospholipase_C&oldid=1170655893 |work=Wikipedia |access-date=2023-11-29 |language=en}}</ref> 
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| [[Cholesterol oxidase]]s || [[Oxidize]]s and isomerizes [[cholesterol]] to cholest-4-en-3-one.<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF09129 |title=Pfam entry: Cholesterol oxidase |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929083056/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF09129 |archive-date=2007-09-29 |url-status=dead }}</ref> || Depletes [[cellular membrane]]s of cholesterol, used in bacterial [[pathogenesis]].||two loops of residue which act as a lid on the [[active site]]<ref>{{Cite journal |last1=Yue |first1=Q. Kimberley |last2=Kass |first2=Ignatius J. |last3=Sampson |first3=Nicole S. |last4=Vrielink |first4=Alice |date=1999-04-01 |title=Crystal Structure Determination of Cholesterol Oxidase from Streptomyces and Structural Characterization of Key Active Site Mutants |url=https://pubs.acs.org/doi/10.1021/bi982497j |journal=Biochemistry |language=en |volume=38 |issue=14 |pages=4277–4286 |doi=10.1021/bi982497j |pmid=10194345 |issn=0006-2960}}</ref>
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| [[Carotenoid oxygenase]]|| Cleaves [[carotenoids]].<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF03055 |title=Pfam entry: Retinal pigment epithelial membrane protein |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929104832/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF03055 |archive-date=2007-09-29 |url-status=dead }}</ref>|| Carotenoids function in both plants and animals as [[hormone]]s (includes [[vitamin A]] in humans), [[pigment]]s, [[Flavor (taste)|flavor]]s, floral scents and defense compounds. ||composed of multiple enzymes attached together forming branch-like structures<ref>{{Citation |title=Carotenoid oxygenase |date=2023-11-29 |url=https://en.wikipedia.org/w/index.php?title=Carotenoid_oxygenase&oldid=1187404336 |work=Wikipedia |access-date=2023-11-29 |language=en}}</ref>
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| [[Lipoxygenase]]s || [[Iron]]-containing enzymes that [[catalyze]] the [[Lipoxygenase|dioxygenation]] of polyunsaturated [[fatty acid]]s.<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00305 |title=Pfam entry: Lipoxygenase |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929104653/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00305 |archive-date=2007-09-29 |url-status=dead }}</ref> ||In animals lipoxygenases are involved in the synthesis of [[inflammation|inflammatory]] mediators known as [[leukotrienes]].|| hundreds of [[amino acid]]s that makes up a protein are organized into two domains: beta-sheet N terminal and helical C terminal<ref>{{Cite journal |last1=Prigge |first1=S. T. |last2=Boyington |first2=J. C. |last3=Faig |first3=M. |last4=Doctor |first4=K. S. |last5=Gaffney |first5=B. J. |last6=Amzel |first6=L. M. |date=1997-11-01 |title=Structure and mechanism of lipoxygenases |journal=Biochimie |volume=79 |issue=11 |pages=629–636 |doi=10.1016/S0300-9084(97)83495-5 |issn=0300-9084|doi-access=free |pmid=9479444 }}</ref>
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| [[Clostridium perfringens alpha toxin|Alpha toxin]]s || Cleave [[phospholipid]]s in the cell membrane, similar to Phospholipase C.<ref>[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1kho PDBsum entry: Alpha Toxin]</ref>|| Bacterial pathogenesis, particularly by ''[[Clostridium perfringens]]''. ||soluble monomer with oligomeric pre-pore complexes<ref>{{Cite web |title=Alpha Toxin - an overview {{!}} ScienceDirect Topics |url=https://www.sciencedirect.com/topics/nursing-and-health-professions/alpha-toxin |access-date=2023-11-29 |website=www.sciencedirect.com}}</ref>
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| [[Sphingomyelinase]] C || A [[phosphodiesterase]], cleaves phosphodiester bonds.<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF01663 |title=Pfam entry: Type I phosphodiesterase |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929084034/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF01663 |archive-date=2007-09-29 |url-status=dead}}</ref> || Processing of lipids such as [[sphingomyelin]].||[[Saposin protein domain|saposin]] domain and connector regions with a metallophosphate catalytic domain <ref>{{Cite journal |last1=Xiong |first1=Zi-Jian |last2=Huang |first2=Jingjing |last3=Poda |first3=Gennady |last4=Pomès |first4=Régis |last5=Privé |first5=Gilbert G. |date=2016-07-31 |title=Structure of Human Acid Sphingomyelinase Reveals the Role of the Saposin Domain in Activating Substrate Hydrolysis |url=https://www.sciencedirect.com/science/article/pii/S0022283616302200 |journal=Journal of Molecular Biology |volume=428 |issue=15 |pages=3026–3042 |doi=10.1016/j.jmb.2016.06.012 |pmid=27349982 |issn=0022-2836}}</ref>
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| [[Glycosyltransferase]]s: MurG and Transglycosidases || Catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming [[glycosidic]] bonds.<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00534 |title=Pfam entry: Glycosyl transferases group 1 |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929120820/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00534 |archive-date=2007-09-29 |url-status=dead }}</ref> || Biosynthesis of [[disaccharide]]s, [[oligosaccharide]]s and [[polysaccharide]]s (glycoconjugates), MurG is involved in bacterial [[peptidoglycan]] biosynthesis. || three glycine rich loops: one in the C terminal and two in the N terminal <ref>{{Cite journal |last1=Ünligil |first1=Uluğ M |last2=Rini |first2=James M |date=2000-10-01 |title=Glycosyltransferase structure and mechanism |url=https://www.sciencedirect.com/science/article/pii/S0959440X0000124X |journal=Current Opinion in Structural Biology |volume=10 |issue=5 |pages=510–517 |doi=10.1016/S0959-440X(00)00124-X |pmid=11042447 |issn=0959-440X}}</ref> 
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| [[Ferrochelatase]] || Converts [[protoporphyrin IX]] into [[heme]].<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00762 |title=Pfam entry: Ferrochelatase |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929120511/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00762 |archive-date=2007-09-29 |url-status=dead }}</ref> || Involved in [[porphyrin]] metabolism, [[protoporphyrin]]s are used to strengthen [[egg shell]]s. || [[polypeptide]] folded into two domains that each have a four-stranded parallel [[beta sheet]] flanked by alpha [[A-helices|helices]]<ref>{{Cite journal |last1=Al-Karadaghi |first1=Salam |last2=Hansson |first2=Mats |last3=Nikonov |first3=Stanislav |last4=Jönsson |first4=Bodil |last5=Hederstedt |first5=Lars |date=November 1997 |title=Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis |journal=Structure |volume=5 |issue=11 |pages=1501–1510 |doi=10.1016/s0969-2126(97)00299-2 |issn=0969-2126|doi-access=free |pmid=9384565 }}</ref>
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| Myotubularin-related protein family || Lipid [[phosphatase]] that dephosphorylates [[Phosphatidylinositol 3-phosphate|PtdIns3P]] and [[Phosphatidylinositol (3,5)-bisphosphate|PtdIns(3,5)P2]].<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF06602 |title=Pfam entry:Myotubularin-related |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070926215455/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF06602 |archive-date=2007-09-26 |url-status=dead }}</ref>|| Required for [[muscle]] cell differentiation. ||contains a [[GRAM domain]], [[SET domain|SET]] interacting domain, and a [[PDZ domain|PDZ]] binding domain<ref>{{Cite book |title=Emery and Rimoin's Principles and Practice of Medical Genetics |url=https://www.sciencedirect.com/book/9780123838346/emery-and-rimoins-principles-and-practice-of-medical-genetics |access-date=2023-11-29 |isbn=978-0-12-383834-6 |language=en}}</ref>
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| [[Dihydroorotate dehydrogenase]]s || [[Oxidation]] of dihydroorotate (DHO) to orotate.<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF01180 |title=Pfam entry:Dihydroorotate dehydrogenase |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070926220055/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF01180 |archive-date=2007-09-26 |url-status=dead }}</ref>|| Biosynthesis of [[pyrimidine]] [[nucleotide]]s in [[prokaryotic]] and [[eukaryotic]] cells. ||composed of two domains: [[Alpha beta barrel|alpha/beta barrel]] domain that contains the active site and an [[alpha-helical]] domain that forms the opening tunnel to the active site <ref>{{Cite journal |last1=Liu |first1=Shenping |last2=Neidhardt |first2=Edie A |last3=Grossman |first3=Trudy H |last4=Ocain |first4=Tim |last5=Clardy |first5=Jon |date=January 2000 |title=Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents |journal=Structure |volume=8 |issue=1 |pages=25–33 |doi=10.1016/s0969-2126(00)00077-0 |issn=0969-2126|doi-access=free |pmid=10673429 }}</ref>
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|[[Glycolate oxidase]] || Catalyses the [[oxidation]] of α-[[hydroxycarboxylic acid]]s to the corresponding α-[[ketoacid]]s.<ref>{{Cite web |url=http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF01070 |title=Pfam entry: FMN-dependent dehydrogenase |access-date=2007-01-25 |archive-url=https://web.archive.org/web/20070929111635/http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF01070 |archive-date=2007-09-29 |url-status=dead }}</ref>|| In green [[plant]]s, the enzyme participates in [[photorespiration]]. In animals, the enzyme participates in production of [[oxalate]].||β8/α8 fold containing alpha helices, beta strands, and loops and turns<ref>{{Cite web |title=Glycolate oxidase - Proteopedia, life in 3D |url=https://proteopedia.org/wiki/index.php/Glycolate_oxidase#:~:text=The%20biological%20assembly%20of%20human,are%20shown%20as%20red%20spheres. |access-date=2023-11-28 |website=proteopedia.org |language=en}}</ref>
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