cite journal author Sun JP, Zhang ZY, Wang WQ title An overview of the proteintyrosinephosphatase ... ref Links to all 107 members of the proteintyrosinephosphatase family can be found in the template Proteintyrosine phosphatases template at the bottom of this article. Class I The class I PTPs ... of enzymes with both Ser Thr EC number 3.1.3.16 and tyrosine specific proteinphosphatase EC ... structure of human receptor proteintyrosinephosphatase kappa phosphatase domain 1 journal Protein ... N, Johnson MR, Perkins LA, Melnick MB title The nonreceptor proteintyrosinephosphatase corkscrew ... , PDB2 1jf8 , PDB2 1jfv , PDB2 1jl3 , PDB2 1ljl Pfam box Symbol Y phosphatase Name Proteintyrosinephosphatase image PDB 1ypt EBI.jpg caption Structure of Yersinia proteintyrosinephosphatase. ref ... MA title Crystal structure of Yersinia proteintyrosinephosphatase at 2.5 A and the complex with tungstate ... Symbol Y phosphatase2 Name Proteintyrosinephosphatase, SIW14 like image PDB 1xri EBI.jpg caption ... Name Proteintyrosinephosphatase like, PTPLA Pfam PF04387 InterPro IPR007482 PROSITE PDB Expression ... TyrosinePhosphatase EC number 3.1.3.48 Phosphatases Proteintyrosine phosphatases Intracellular ...Expert subject date May 2010 Proteintyrosine phosphatases PTPs are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Proteintyrosine pTyr phosphorylation ..., maintaining an appropriate level of proteintyrosine phosphorylation is essential for many cellular functions. Tyrosine specific protein phosphatases PTPase EC number 3.1.3.48 catalyse ... JM title Proteintyrosine phosphatases mechanisms of catalysis and regulation journal Curr Opin Chem ... S, Lombroso PJ title Receptor and nonreceptor proteintyrosine phosphatases in the nervous system ... cite journal author Alonso A, Sasin J, et al. title Proteintyrosine phosphatases in the human genome ... PTPs 21 receptor tyrosinephosphatase 17 nonreceptor type PTPs 61 VH 1 like or dual specific phosphatases ... more details
PBB geneid 640 Tyrosineprotein kinase BLK also known as B lymphocyte kinase is an enzyme that in humans ... homologue of a B lymphocyte specific proteintyrosine kinase blk journal Oncogene volume 10 issue ... The tyrosineprotein kinase BLK has been shown to Proteinprotein interaction interact with UBE3A ... tyrosine kinase related to murine Blk. journal J. Immunol. volume 154 issue 3 pages 1265 72 year 1995 pmid 7822795 doi cite journal author Donovan JA, Wange RL, Langdon WY, Samelson LE title The protein product of the c cbl protooncogene is the 120 kDa tyrosine phosphorylated protein in Jurkat cells ... of sites on the Src family proteintyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C gamma 2, microtubule associated protein kinase, GTPase activating protein, and phosphatidylinositol 3 kinase. journal Mol. Cell. Biol. volume 13 issue 9 pages ... P, et al. title In vivo and in vitro specificity of proteintyrosine kinases for immunoglobulin G ... BLK B lymphoid tyrosine kinase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 640 accessdate ref The PBB Summary template is automatically maintained by Protein ... family tyrosine kinase Blk through E6AP mediated ubiquitination journal Proc. Natl. Acad. Sci. U.S.A. ... author Dymecki SM, Niederhuber JE, Desiderio SV title Specific expression of a tyrosine kinase gene ... of Src family tyrosine kinases regulates functional interaction with a B cell substrate. journal ... mouse protein that interacts with Bcl 2 and Bcl xL, is a potent death agonist. journal J. Biol ... journal author Oda H, Kumar S, Howley PM title Regulation of the Src family tyrosine kinase Blk through ... 279 issue 19 pages 19512 22 year 2004 pmid 14970218 doi 10.1074 jbc.M309074200 refend gene 8 stub Tyrosine kinases The PBB Controls template provides controls for Protein Box Bot, please see Template PBB Controls for details. PBB Controls update page yes require manual inspection no update protein box ... more details
Protein serine threonine phosphatase PSP ref name pmid19879837 cite journal author Shi Y title Serine threonine phosphatases mechanism through structure journal Cell volume 139 issue 3 pages 468 84 year 2009 month October pmid 19879837 doi 10.1016 j.cell.2009.10.006 url http linkinghub.elsevier.com retrieve pii S0092 8674 09 01254 9 ref is a form of phosphoprotein phosphatase that acts upon serine threonine residues. Serine and threonine phosphates are stable under physiological conditions, so a phosphatase has to remove the phosphate to reverse the regulation. Ser Thr specific protein phosphatases are regulated by their location within the cell biology cell and by specific Enzyme inhibitor inhibitor proteins. Examples There are several known groups with numerous members in each PPP1 , , 1, 2 ProteinPhosphatase 2 PPP2 formerly 2A Calcineurin PPP3 formerly 2b, also known as calcineurin PPP2C PPP4C PPP4 PPP5C PPP5 PPP6C PPP6 links are to the catalytic subunit All but PPP2C have sequence homology in the enzyme catalytic domain protein domain , but differ in substrate specificity. Citation needed date November 2008 References reflist External links EC number 3.1.3.16 Esterases Intracellular signaling peptides and proteins Category Enzymes biochem stub ... more details
Phospho proteinphosphatase 1 PP1 belongs to a certain class of phosphatases known as protein serine threonine phosphatases. This type of phosphatase includes metal dependent protein phosphatases PPMs ... PPP1R6, a novel member of the family of glycogen targetting subunits of proteinphosphatase 1 journal ... Structural basis for the recognition of regulatory subunits by the catalytic subunit of proteinphosphatase ... s. Regulation of HIV 1 Transcription genetics transcription by ProteinPhosphatase 1 PP1 . It has been recognized that proteinphosphatase 1 PP1 serves as an important regulator of HIV 1 transcription ... et. al. title Regulation of HIV 1 transcription by proteinphosphatase 1 journal Current HIV ... Information protein Name PPP1CA proteinphosphatase 1, catalytic subunit, alpha isozyme width ... 13 LocusSupplementaryData protein Name PPP1CB proteinphosphatase 1, catalytic subunit, beta isozyme ... p Band 23 LocusSupplementaryData protein Name PPP1CC proteinphosphatase 1, catalytic subunit, gamma ... Proteinphosphatase 1 targeted in many directions journal J. Cell. Sci. volume 115 issue Pt 2 pages ... MeshName ProteinPhosphatase 1 Category EC 3.1.3 ... 9312013 doi 10.1093 emboj 16.18.5537 pmc 1170186 ref cell division, apoptosis , protein synthesis, and regulation ... sites on protein targeting to glycogen for enzymes of glycogen metabolism journal The Journal of Biological ..., P, Nairn, AC, Kuriyan, J title Three dimensional structure of the catalytic subunit of protein serine threonine phosphatase 1 journal Nature date 1995 08 31 volume 376 issue 6543 pages 745 53 pmid 7651533 doi 10.1038 376745a0 ref The catalytic subunit consists of a 30 kD single domain protein that can ... of protein phosphatases insights into catalysis and regulation journal Annual review of biophysics ... phosphatase specific for the C terminal domain of RNA polymerase II, in complex with a transition ... protein phosphatases journal The Biochemical journal date 1995 10 01 volume 311 pages 17 29 ... more details
phosphatase PPP family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the proteinphosphatase Mg sup 2 sup or Mn sup 2 sup dependent PPM family, composed primarily of PP2C. The protein Tyr phosphatase PTP super family forms the second group, and the aspartate based protein ... based upon their substrate specificity. class wikitable Class Example Substrate Reference Tyrosine specific phosphatases PTP1B Phospho Tyrosine ref cite journal author Zhang ZY title Proteintyrosine ... bst0320343.htm ref Serine Threonine PP PPM PPP families main Protein serine threonine phosphataseProtein ...A phosphatase is an enzyme that removes a phosphate group from its Substrate biochemistry substrate by Hydrolysis ... molecules like adenosine triphosphate ATP . A common phosphatase in many organisms is alkaline phosphatase . Protein phosphorylation is the most common and important form of reversible protein posttranslational modification PTM , with up to 30 of all proteins being phosphorylated at any given time. Protein ..., protein phosphatases PPs are the primary effectors of dephosphorylation and can be grouped into three ... of the protein serine threonine phosphatases journal Trends Biochem. Sci. volume 21 issue 11 ... of Tyrosine dephosphorylation by a CDP The free cysteine nucleophile forms a bond with the phosphorus atom of the phosphate moiety, and the P O bond linking the phosphate group to the tyrosine is protonated ... Mumby MC, Walter G title Protein serine threonine phosphatases structure, regulation, and functions ... VHR, DUSP1 to DUSP28 Phospho Tyrosine Serine Threonine ref cite journal author Camps M, Nichols ... www.fasebj.org cgi pmidlookup?view long&pmid 10627275 ref Histidine Phosphatase PHP Phospho Histidine ref cite journal author B umer N, M urer A, Krieglstein J, Klumpp S title Expression of protein histidine phosphatase in Escherichia Coli , purification, and determination of enzyme activity journal ... Lipid Phosphatase PTEN gene PTEN Phosphatidyl Inositol 3,4,5 Triphosphate ref cite journal doi 10.1042 ... more details
processes. It functions as a receiver of phosphate groups that are transferred by way of protein kinase s so called receptor tyrosine kinase s . Phosphorylation of the hydroxyl group changes the activity of the target protein. A tyrosine residue also plays an important role in photosynthesis ... by protein kinase s. In its phosphorylated state, it is referred to as phosphotyrosine . Tyrosine ... markers meta , ortho tyrosine and DOPA in cataractous lenses is accompanied by a lower protein and phenylalanine ... 200 ImageName Skeletal formula of the L isomer ImageFile1 L Tyrosine zwitterion 3D balls.png ImageSize1 200px ImageName1 Ball and stick model of the L isomer as a zwitterion IUPACName S Tyrosine OtherNames ... Tyrosine abbreviated as Tyr or Y ref cite web author IUPAC IUBMB Joint Commission on Biochemical Nomenclature ... by cell biology cells to protein biosynthesis synthesize protein s. Its codon s are UAC and UAU. It is a non essential amino acid with a polar side group. The word tyrosine is from the Greek language ... Liebig in the protein casein from cheese. ref name urltyrosine Infoplease.com cite web url http www.infoplease.com ce6 sci A0849873.html title Tyrosine author authorlink coauthors year 2007 work The Columbia ... cite web url http www.etymonline.com index.php?term tyrosine title Tyrosine author Douglas Harper ... group or side chain. Functions Aside from being a proteinogenic amino acid, tyrosine has a special ... reduced in the photosystem II by the four core manganese clusters. Dietary sources Tyrosine, which can also be synthesized in the body from phenylalanine , is found in many high protein food ... , and sesame seed s. ref cite web title Tyrosine url http www.umm.edu altmed articles tyrosine 000329.htm work University of Maryland Medical Center accessdate 2011 03 17 ref Tyrosine can also be obtained through supplementation. Biosynthesis Image Tyrosine biosynthesis2.png thumb center 400px Plant biosynthesis of tyrosine from shikimic acid . In plants and most microorganisms, tyr is produced ... more details
MAPK phosphatases are a class of phosphatase s. They are involved in MAP kinase signaling. ref MeshName MAPK Phosphatases ref References reflist Proteintyrosine phosphatases Intracellular signaling peptides and proteins MAP kinase activation Category Cell signaling Category Enzymes Category Protein kinases ... more details
Dual specificity phosphatase is a form of phosphatase that can act upon tyrosine or serine threonine residues. ref MeshName Dual Specificity Phosphatases ref References reflist Intracellular signaling peptides and proteins Proteintyrosine phosphatases Category Enzymes biochem stub ... more details
Proteintyrosinephosphatase main Proteintyrosinephosphatase CDC14s CDC14A , CDC14B , CDC14C , CDKN3 Phosphatase and tensin homologs PTEN gene PTEN slingshot SSH1 , SSH2 , SSH3 Dual specificity phosphatase main Dual specificity phosphatase DUSP1 , DUSP2 , DUSP3 , DUSP4 , DUSP5 , DUSP6 , DUSP7 , DUSP8 ... phosphatase activity include Protein serine threonine phosphatase main Protein serine threonine phosphatase ...Phosphoprotein phosphatase is an enzyme that dephosphorylates certain phosphorylated proteins. ref name Lewin2007 cite book author Benjamin Lewin title Cells url http books.google.com books?id 2VEGC8j9g9wC&pg PA625 accessdate 20 December 2010 year 2007 publisher Jones & Bartlett Learning isbn 9780763739058 pages 625 ref In some contexts, Phosphoprotein phosphatase is equated with serine threonine specific proteinphosphatase , and classified under EC number 3.1.3.16 . ref name urlENZYME entry 3.1.3.16 cite web url http www.expasy.org cgi bin nicezyme.pl?3.1.3.16 title ENZYME entry 3.1.3.16 format work accessdate 2010 12 20 ref In other contexts, the term also includes proteintyrosinephosphatase EC number 3.1.3.48 and dual specificity phosphatase . ref name Roskoski1996 cite book author Robert Roskoski title Biochemistry url http books.google.com books?id 2EqyT2rnRKEC&pg PA430 accessdate 20 December 2010 year 1996 publisher Elsevier Health Sciences isbn 9780721651743 pages 430 ref ref name Lewin2007 cite book author Benjamin Lewin title Cells url http books.google.com books?id 2VEGC8j9g9wC&pg PA626 accessdate 20 December 2010 year 2007 publisher Jones & Bartlett Learning isbn 9780763739058 ... ions to serine , threonine and tyrosine residues in the enzyme. This addition is catalysed by protein kinase s. The reverse reaction is carried out by phosphatase. Effects of activation of phosphoprotein phosphatase Phosphoprotein phosphatase is activated by the hormone insulin, which indicates ... MeshName Phosphoprotein phosphatase Category Enzymes Enzyme stub Phosphatases Intracellular signaling ... more details
dablink Tyrosine kinases are a subclass of protein kinase , see there for the principles of protein phosphorylation Pfam box Symbol Pkinase Tyr Name Proteintyrosine kinase image PDB 1m61 EBI.jpg width caption Tyrosineprotein kinase zap 70 Pfam PF07714 InterPro IPR001245 SMART TyrKc Prosite PDOC00629 SCOP 1apm TCDB CDD cd00192 OPM family 207 OPM protein 2k1k PDB A tyrosine kinase is an enzyme that can ... tyrosine on the protein. Tyrosine kinases are a subgroup of the larger class of protein kinase s which ... , are often effective cancer treatments. Most tyrosine kinases have an associated proteintyrosinephosphatase , which removes the phosphate group. Reaction Protein kinases are a group of enzymes that possess ... of the protein that they are contained in. ref name Lehninger 2008 Phosphorylation at tyrosine ... a possible role for proteintyrosine kinase journal Br. J. Pharmacol. volume 122 issue 1 pages 59 ... fundamental in the normal survival of a living organism. Proteintyrosine kinase plays a role in this task, too. A proteintyrosine kinase called PTK2 pp125 is likely at hand in the influence of cellular ... RR, Reynolds AB, Parsons JT title pp125FAK a structurally distinctive proteintyrosine kinase associated ... in cellular focal adhesions. The proteintyrosine kinase pp125 is one of the major phosphotyrosine ... unique, meaning it could be a new member of the proteintyrosine kinase family. This proteintyrosine kinase is up to about 70 unique compared to some other proteintyrosine kinases, a figure that is unlike those between actual members of an established proteintyrosine kinase family. ref name ... with the cytoplasm, dubbing it one in a large group of cytoplasmic proteintyrosine kinases. ref ... protein to the total tyrosine kinase activity within the nuclear matrix is unknown, however because ... in rats, where the effects of inhibitors tyrphostin and genistein are involved with proteintyrosine ... by a protein, called a ligand. A number of receptor tyrosine kinases, though certainly not all, do ... more details
and enzymology of proteintyrosine O sulfation journal J. Biol. Chem. volume 278 issue 27 pages 24243 ...Tyrosine sulfation is a posttranslational modification where a sulfate group is added to a tyrosine residue of a protein molecule. Secreted proteins and extracellular parts of membrane proteins that pass through the Golgi apparatus may be sulfated. Sulfation was first discovered by Frederick Bettelheim Bettelheim in bovine fibrinopeptide B in 1954 ref Tyrosine O sulfate in a peptide from fibrinogen. F. R. Bettelheim, J. Am. Chem. Soc., 1954, 76 10 , pp 2838 2839, doi 10.1021 ja01639a073 ref and later found be present in animals and plants but not in prokaryote s or in yeast. Function Sulfation plays role in strengthening proteinprotein interactions. Types of human proteins known to undergo tyrosine sulfation include adhesion molecules, G protein coupled receptors, coagulation factors, serine protease inhibitor s, extracellular matrix proteins, and hormones. Tyrosine O sulfate is a stable molecule and is excreted in urine in animals. No enzymatic mechanism of tyrosine sulfate desulfation is known to exist. By knock out of TPST genes in mice, it may be observed that tyrosine sulfation ... phosphosulfate PAPS to the side chain hydroxyl group of a tyrosine residue. Sulfation sites are tyrosine residues exposed on the surface of the protein typically surrounded by acidic residues, a detailed ... genes are subject to transcriptional regulation and tyrosine O sulfate is very stable and cannot be easily degraded by mammalian sulfatases. Tyrosine O sulfation is an irreversible process in vivo . Antibody for detection of tyrosine sulfated epitopes In 2006, an article was published in the Journal ... 24243 cite journal author Hoffhines AJ title Detection and purification of tyrosine sulfated proteins ... first3 KG last4 Leary first4 JA last5 Moore first5 KL pmc 1764208 Protein primary structure DEFAULTSORT Tyrosine Sulfation Category Posttranslational modification ja ... more details
enzyme Name tyrosine 2,3 aminomutase EC number 5.4.3.6 CAS number 9073 38 5 IUBMB EC number 5 4 3 6 GO code 0050368 image width caption Orphan date April 2009 Refimprove date April 2009 In enzymology , a tyrosine 2,3 aminomutase EC number 5.4.3.6 is an enzyme that catalysis catalyzes the chemical reaction L tyrosine math rightleftharpoons math 3 amino 3 4 hydroxyphenyl propanoate Hence, this enzyme has one substrate biochemistry substrate , L tyrosine , and one product chemistry product , 3 amino 3 4 hydroxyphenyl propanoate . This enzyme belongs to the family of isomerase s, specifically those intramolecular transferase s transferring amino groups. The systematic name of this enzyme class is L tyrosine 2,3 aminomutase . This enzyme is also called tyrosine alpha,beta mutase . This enzyme participates in tyrosine metabolism . It employs one cofactor, 5 methylene 3,5 dihydroimidazol 4 one MIO which is formed autocatalytic rearrangement of the internal tripeptide Ala Ser Gly. Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 2OHY . References reflist 1 cite journal author Kurylo Borowska Z, Abramsky T date 1972 title Biosynthesis of tyrosine journal Biochim. Biophys. Acta. volume 264 pages 1&ndash 10 pmid 5021987 issue 1 Category EC 5.4.3 Category Enzymes of known structure isomerase stub ... more details
name pmid9626667 Tyrosine hydroxylase activity is regulated chronically days by protein synthesis ... phosphorylation of brain tyrosine hydroxylase by cyclic AMP dependent protein kinase mechanism ...PBB geneid 7054 Tyrosine hydroxylase or tyrosine 3 monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L tyrosine small L small tyrosine to L DOPA small L small 3,4 ... Tyrosine hydroxylase journal Adv. Enzymol. Relat. Areas Mol. Biol. volume 70 issue pages 103 220 year ... Tyrosine hydroxylase human isoforms, structure and regulation in physiology and pathology journal ... neurotransmitters norepinephrine noradrenaline and epinephrine adrenaline . Tyrosine hydroxylase catalyzes the rate limiting step in this synthesis of catecholamines . In humans, tyrosine ... nervous system CNS , peripheral symphatic neurons and the adrenal medulla . ref name pmid8822146 Tyrosine ... table align left tr td Infobox enzyme Name tyrosine 3 monooxygenase EC number 1.14.16.2 CAS number 9036 22 0 IUBMB EC number 1 14 16 2 GO code 0004511 image Tyrosine to L DOPA reaction TH.svg width caption Tyrosine hydroxylase catalyzes conversion of tyrosine to L DOPA small L small DOPA using Fe sup 2 sup , O sub 2 sub and BH sub 4 sub td td td tr table Tyrosine hydroxylase catalysis catalyzes the reaction where small L small tyrosine is hydroxylation hydroxylated in the Meta ... atoms in O sub 2 sub is used to hydroxylate the tyrosine molecule to obtain small L small ... AAAHs , tyrosine hydroxylase use the cofactor tetrahydrobiopterin BH sub 4 sub under normal conditions, although other similar molecules may also work as a cofactor for tyrosine hydroxylase. ref ... subunits in tyrosine hydroxylase is coordinated with an iron II atom presented in the active site. The oxidation ... and adrenaline, tyrosine hydroxylase is therefore found in the cytosol of all cells containing these catecholamines . This initial reaction catalyzed by tyrosine hydroxylase has been shown to be the rate ... more details
doi url issn ref In humans, the tyrosine aminotransferase protein is encoded by the TAT gene . A deficiency ... diagram of the tyrosine aminotransferase protein dimer dimer . The prosthetic group PLP is visible in both ...enzyme Name Tyrosine transaminase EC number 2.6.1.5 CAS number 9014 55 5 IUBMB EC number 2 6 1 5 GO code 0080130 image 3DYD.png width caption Human tyrosine aminotransferase rainbow colored, N terminus ... 3DYD cite journal author Karlberg T, Moche M, Andersson J, et al. title Human tyrosine aminotransferase journal To be Published volume issue pages year 2008 month pmid doi url issn ref protein Name Human tyrosine aminotransferase caption image width 275 HGNCid 11573 Symbol TAT AltSymbols EntrezGene ... 22.1 LocusSupplementaryData Tyrosine aminotransferase or tyrosine transaminase is an enzyme present in the liver and catalyzes the conversion of tyrosine to 4 hydroxyphenylpyruvate . ref name pmid1349265 cite journal author Dietrich JB title Tyrosine aminotransferase a transaminase among others? journal ... of tyrosine as a result of tyrosine failing to undergo an aminotransferase reaction ... H, Scherer G title Isolation and characterization of the human tyrosine aminotransferase gene ... in chemical reaction catalyzed by the tyrosine aminotransferase enzyme are shown below the amino acid tyrosine , the prosthetic group pyridoxal phosphate , and the resulting product 4 hydroxyphenylpyruvic ... 2004 month pmid 15264254 doi 10.1002 jcc.20084 url issn ref Each side of the dimer protein includes pyridoxal pyruvate PLP bonded to the Lys280 residue of the tyrosine aminotransferase molecule. The amine group of tyrosine attacks the alpha carbon of the imine bonded to Lys280, forming a tetrahedral ... as the base that attacks the tyrosine in transimination. The electrons left behind from the loss ... orientation Tyrosine Aminotransferase as a dimer has two identical active sights. Lys280 is attached ... TATActivesite.jpg Pathology Tyrosinemia is the most common metabolic disease associated with tyrosine ... more details
enzyme Name phosphorylase phosphatase EC number 3.1.3.17 CAS number 9025 74 5 IUBMB EC number 3 1 3 17 GO code 0050196 image width caption In enzymology , a phosphorylase phosphatase EC number 3.1.3.17 is an enzyme that catalysis catalyzes the chemical reaction phosphorylase a 4 H sub 2 sub O math rightleftharpoons math 2 phosphorylase b 4 phosphate Thus, the two substrate biochemistry substrates of this enzyme are phosphorylase a and water H sub 2 sub O , whereas its two product chemistry products are phosphorylase b and phosphate . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester monoester bonds. The systematic name of this enzyme class is phosphorylase a phosphohydrolase . Other names in common use include PR enzyme , phosphorylase a phosphatase , glycogen phosphorylase phosphatase , proteinphosphatase C , and type 1 proteinphosphatase . References reflist 1 cite journal author Brandt H, Capulong ZL, Lee EY date 1975 title Purification and properties of rabbit liver phosphorylase phosphatase journal J. Biol. Chem. volume 250 pages 8038&ndash 44 pmid 240850 issue 20 cite journal author GRAVES DJ, FISCHER EH, KREBS EG date 1960 title Specificity studies on muscle phosphorylase phosphatase journal J. Biol. Chem. volume 235 pages 805&ndash 9 pmid 13829077 cite journal author RALL TW, WOSILAIT WD, SUTHERLAND EW date 1956 title The interconversion of phosphorylase a and phosphorylase b from dog heart muscle journal Biochim. Biophys. Acta. volume 20 pages 69&ndash 76 pmid 13315351 doi 10.1016 0006 3002 56 90264 5 issue 1 DEFAULTSORT Phosphorylase phosphatase Category EC 3.1.3 Category Enzymes of unknown structure hydrolase stub ... more details
enzyme Name phosphoglycolate phosphatase EC number 3.1.3.18 CAS number 9025 76 7 IUBMB EC number 3 1 3 18 GO code 0008967 image width caption In enzymology , a phosphoglycolate phosphatase EC number 3.1.3.18 is an enzyme that catalysis catalyzes the chemical reaction 2 phosphoglycolate H sub 2 sub O math rightleftharpoons math glycolate phosphate Thus, the two substrate biochemistry substrates of this enzyme are 2 phosphoglycolate and water H sub 2 sub O , whereas its two product chemistry products are glycolate and phosphate . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester monoester bonds. The systematic name of this enzyme class is 2 phosphoglycolate phosphohydrolase . Other names in common use include phosphoglycolate hydrolase , 2 phosphoglycolate phosphatase , P glycolate phosphatase , and phosphoglycollate phosphatase . This enzyme participates in glyoxylate and dicarboxylate metabolism . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1TE2 , PDB link 1WR8 , PDB link 2HDO , PDB link 2HI0 , and PDB link 2NYV . References reflist 1 cite journal author Christeller JT, Tolbert NE date 1978 title Phosphoglycolate phosphatase. Purification and properties journal J. Biol. Chem. volume 253 pages 1780&ndash 5 pmid 204630 issue 6 hydrolase stub Category EC 3.1.3 Category Enzymes of known structure ... more details
enzyme Name phosphatidate phosphatase EC number 3.1.3.4 CAS number 9025 77 8 IUBMB EC number 3 1 3 4 GO code 0008195 image width caption In enzymology , a phosphatidate phosphatase EC number 3.1.3.4 is an enzyme that catalysis catalyzes the chemical reaction ref name pmid13475370 cite journal author Smith SW, Weiss SB, Kennedy EP title The enzymatic dephosphorylation of phosphatidic acids journal J. Biol. Chem. volume 228 issue 2 pages 915 22 year 1957 month October pmid 13475370 doi url issn ref a 3 sn phosphatidate H sub 2 sub O math rightleftharpoons math a 1,2 diacyl sn glycerol phosphate Thus, the two substrate biochemistry substrates of this enzyme are phosphatidic acid 3 sn phosphatidate and water H sub 2 sub O , whereas its two product chemistry products are diglyceride 1,2 diacyl sn ... phosphatidate phosphohydrolase . Other names in common use include phosphatidic acid phosphatase PAP , acid phosphatidyl phosphatase, phosphatidic acid phosphohydrolase, phosphatidate phosphohydrolase ... GS title Roles of phosphatidate phosphatase enzymes in lipid metabolism journal Trends Biochem. Sci ... beside phosphatidate therefore are also known as lipid phosphate phosphatase . Their main role is in lipid ... phosphatases include PPAP2A LPP1 phosphatidic acid phosphatase type 2A PPAP2B LPP3 phosphatidic acid phosphatase type 2B PPAP2C LPP2 phosphatidic acid phosphatase type 2C PPAPDC1A PPC1A phosphatidic acid phosphatase type 2 domain containing 1A PPAPDC1B PPC1B phosphatidic acid phosphatase type 2 domain containing 1B PPAPDC2 phosphatidic acid phosphatase type 2 domain containing 2 PPAPDC3 phosphatidic acid phosphatase type 2 domain containing 3 LPPR2 lipid phosphate phosphatase related protein type 2 LPPR3 lipid phosphate phosphatase related protein type 3 LPPR4 lipid phosphate phosphatase related protein type 4 LPIN1 lipin 1 ref name pmid16467296 cite journal author Han GS, Wu WI, Carman GM title The Saccharomyces cerevisiae Lipin homolog is a Mg2 dependent phosphatidate phosphatase ... more details
enzyme Name bisphosphoglycerate phosphatase EC number 3.1.3.13 CAS number 9033 04 9 IUBMB EC number 3 1 3 13 GO code 0004083 image width caption In enzymology , a bisphosphoglycerate phosphatase EC number 3.1.3.13 is an enzyme that catalysis catalyzes the chemical reaction 2,3 bisphospho D glycerate H sub 2 sub O math rightleftharpoons math 3 phospho D glycerate phosphate Thus, the two substrate biochemistry substrates of this enzyme are 2,3 bisphospho D glycerate and water H sub 2 sub O , whereas its two product chemistry products are 3 phospho D glycerate and phosphate . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester monoester bonds. The systematic name of this enzyme class is 2,3 bisphospho D glycerate 2 phosphohydrolase . Other names in common use include 2,3 diphosphoglycerate phosphatase , diphosphoglycerate phosphatase , 2,3 diphosphoglyceric acid phosphatase , 2,3 bisphosphoglycerate phosphatase , and glycerate 2,3 diphosphate phosphatase . This enzyme participates in glycolysis gluconeogenesis . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1YFK , PDB link 1YJX , PDB link 2F90 , PDB link 2H4X , PDB link 2H4Z , PDB link 2H52 , and PDB link 2HHJ . References reflist 1 cite journal author JOYCE BK, GRISOLIA S date 1958 title Studies on glycerate 2,3 diphosphatase journal J. Biol. Chem. volume 233 pages 350&ndash 4 pmid 13563500 issue 2 cite journal author RAPOPORT S, LUEBERING J date 1951 title Glycerate 2,3 diphosphatase journal J. Biol. Chem. volume 189 pages 683&ndash 94 pmid 14832286 issue 2 hydrolase stub Category EC 3.1.3 Category Enzymes of known structure ... more details
enzyme Name histidinol phosphatase EC number 3.1.3.15 CAS number 9025 79 0 IUBMB EC number 3 1 3 15 GO code 0004401 image width caption In enzymology , a histidinol phosphatase EC number 3.1.3.15 is an enzyme that catalysis catalyzes the chemical reaction L histidinol phosphate H sub 2 sub O math rightleftharpoons math L histidinol phosphate Thus, the two substrate biochemistry substrates of this enzyme are L histidinol phosphate and water H sub 2 sub O , whereas its two product chemistry products are L histidinol and phosphate . This enzyme belongs to the family of hydrolase s, to be specific, those acting on phosphoric ester monoester bonds. The systematic name of this enzyme class is L histidinol phosphate phosphohydrolase . Other names in common use include histidinol phosphate phosphatase , L histidinol phosphate phosphatase , histidinolphosphate phosphatase , HPpase , and histidinolphosphatase . This enzyme participates in histidine metabolism . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2FPR , PDB link 2FPS , PDB link 2FPU , PDB link 2FPW , and PDB link 2FPX . E. coli main hisB In E. coli the enzyme encoded by the gene hisB is a fused imidazoleglycerol phosphate dehydratase and histidinol phosphatase. ref cite pmid 15042344 ref References reflist 1 cite journal author AMES BN date 1957 title The biosynthesis of histidine L histidinol phosphate phosphatase journal J. Biol. Chem. volume 226 pages 583&ndash 93 pmid 13438843 issue 2 hydrolase stub Category EC 3.1.3 Category Enzymes of known structure ... more details
enzyme Name 2 phosphosulfolactate phosphatase EC number 3.1.3.71 CAS number IUBMB EC number 3 1 3 71 GO code 0050532 image width caption In enzymology , a 2 phosphosulfolactate phosphatase EC number 3.1.3.71 is an enzyme that catalysis catalyzes the chemical reaction 2R 2 phospho 3 sulfolactate H sub 2 sub O math rightleftharpoons math 2R 3 sulfolactate phosphate Thus, the two substrate biochemistry substrates of this enzyme are 2R 2 phospho 3 sulfolactate and water H sub 2 sub O , whereas its two product chemistry products are 2R 3 sulfolactate and phosphate . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester monoester bonds. The systematic name of this enzyme class is R 2 phospho 3 sulfolactate phosphohydrolase . Other names in common use include 2R phosphosulfolactate phosphohydrolase , and ComB phosphatase . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1VR0 . References reflist 1 cite journal author Graham DE, Graupner M, Xu H, White RH date 2001 title Identification of coenzyme M biosynthetic 2 phosphosulfolactate phosphatase. A member of a new class of Mg 2 dependent acid phosphatases journal Eur. J. Biochem. volume 268 pages 5176&ndash 88 pmid 11589710 doi 10.1046 j.0014 2956.2001.02451.x issue 19 hydrolase stub Category EC 3.1.3 Category Enzymes of known structure ... more details
Refimprove date April 2010 enzyme Name tyrosine decarboxylase EC number 4.1.1.25 CAS number 9002 09 9 IUBMB EC number 4 1 1 25 GO code 0004837 image width caption In enzymology , a tyrosine decarboxylase EC number 4.1.1.25 is an enzyme that catalysis catalyzes the chemical reaction L tyrosine math rightleftharpoons math tyramine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L tyrosine , and two product chemistry products , tyramine and carbon dioxide . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L tyrosine carboxy lyase tyramine forming . Other names in common use include L tyrosine decarboxylase , L tyrosine apodecarboxylase , and L tyrosine carboxy lyase . This enzyme participates in tyrosine metabolism and alkaloid biosynthesis. It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References Reflist 1 cite journal author McGilvery RW and Cohen PP date 1948 title The decarboxylation of L phenylalanine by Streptococcus faecalis R journal J. Biol. Chem. volume 174 pages 813&ndash 816 pmid 18871240 issue 3 Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure 4.1 enzyme stub ... more details
enzyme Name Pyridoxal phosphatase EC number 3.1.3.74 CAS number IUBMB EC number 3 1 3 74 GO code image width caption In enzymology , a pyridoxal phosphatase EC number 3.1.3.74 is an enzyme that catalysis catalyzes the chemical reaction pyridoxal 5 phosphate H sub 2 sub O math rightleftharpoons math pyridoxal phosphate Thus, the two substrate biochemistry substrates of this enzyme are pyridoxal 5 phosphate and water H sub 2 sub O , whereas its two product chemistry products are pyridoxal and phosphate . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester monoester bonds. The systematic name of this enzyme class is pyridoxal 5 phosphate phosphohydrolase . Other names in common use include vitamine B sub 6 sub pyridoxine phosphatase , PLP phosphatase , vitamin B sub 6 sub phosphate phosphatase , and PNP phosphatase . This enzyme participates in vitamin B sub 6 sub metabolism. Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2CFR , PDB link 2CFS , PDB link 2CFT , PDB link 2OYC , PDB link 2P27 , and PDB link 2P69 . References reflist 1 cite journal author Fonda ML date 1992 title Purification and characterization of vitamin B sub 6 sub phosphate phosphatase from human erythrocytes journal J. Biol. Chem. volume 267 pages 15978&ndash 83 pmid 1322411 issue 22 cite journal author Fonda ML, Zhang YN date 1995 title Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase journal Arch. Biochem. Biophys. volume 320 pages 345&ndash 52 pmid 7625842 doi 10.1016 0003 9861 95 90018 7 issue 2 cite journal author OS date 2003 title Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution journal J. Biol. Chem. volume 278 pages 50040&ndash 6 pmid 14522954 doi 10.1074 jbc.M309619200 last2 Kim first2 DW last3 Kang first3 TC last4 Won first4 MH last5 Baek first5 ... more details
red of the protein dimer dimer ic structure of bacterial alkaline phosphatase. ref name pmid2010919 PDB 1ALK cite journal author Kim EE, Wyckoff HW title Reaction mechanism of alkaline phosphatase based ...enzyme Name Alkaline phosphatase EC number 3.1.3.1 CAS number 9001 78 9 IUBMB EC number 3 1 3 1 GO code ... phosphatase Name Alkaline phosphatase image PDB 1alk EBI.jpg width caption Structure of alkaline phosphatase ... phosphatase based on crystal structures. Two metal ion catalysis journal J. Mol. Biol. volume ... Pfam PF00245 InterPro IPR001952 SMART SM00098 PROSITE PDOC00113 SCOP 1alk TCDB OPM family OPM protein ... phosphatase ALP , ALKP EC number 3.1.3.1 is a hydrolase enzyme responsible for removing phosphate groups ... as basic phosphatase . ref name Tamas2002 cite journal author Tam s L, Huttov J, Mistrk I, Kogan ... doi pmid pmc ref Bacterial In bacterium bacteria , alkaline phosphatase is located in the periplasmic ... variation than the actual interior of the cell, bacterial alkaline phosphatase is comparatively ... phosphate groups for uptake and use, is supported by the fact that alkaline phosphatase is usually produced ... , however, mutant Escherichia coli lacking alkaline phosphatase survive quite well, as do mutants unable to shut off alkaline phosphatase production citation needed date November 2010 ... alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase ... M title Inorganic pyrophosphatase activity of purified bovine pulp alkaline phosphatase at physiological ... isbn 9780121819651 ref Common alkaline phosphatases used in research include Shrimp alkaline phosphatase SAP , from a species of Arctic shrimp Pandalus borealis Calf intestinal alkaline phosphatase CIP Placenta l alkaline phosphatase PALP and its C terminally truncated version that lacks the last ... phosphatase SEAP Alkaline phosphatase has become a useful tool in molecular biology laboratories ..., the alkaline phosphatase from shrimp is the most useful, as it is the easiest to inactivate once ... more details
enzyme Name phosphoserine phosphatase EC number 3.1.3.3 CAS number 9025 73 4 IUBMB EC number 3 1 3 3 GO code 0004647 image width caption In enzymology , a phosphoserine phosphatase EC number 3.1.3.3 is an enzyme that catalysis catalyzes the chemical reaction O phospho L or D serine H sub 2 sub O math rightleftharpoons math L or D serine phosphate The 3 substrate biochemistry substrates of this enzyme are O phospho L serine , O phospho D serine , and water H sub 2 sub O , whereas its 3 product chemistry products are L serine , D serine , and phosphate . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester monoester bonds. The systematic name of this enzyme class is O phosphoserine phosphohydrolase . This enzyme participates in glycine, serine and threonine metabolism . Structural studies As of late 2007, 12 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1F5S , PDB link 1J97 , PDB link 1L7M , PDB link 1L7N , PDB link 1L7O , PDB link 1L7P , PDB link 1L8L , PDB link 1L8O , PDB link 1NNL , PDB link 2J6Y , PDB link 2J6Z , and PDB link 2J70 . References reflist 1 cite journal author BORKENHAGEN LF, KENNEDY EP date 1959 title The enzymatic exchange of L serine with O phospho L serine catalyzed by a specific phosphatase journal J. Biol. Chem. volume 234 pages 849&ndash 53 pmid 13654276 issue 4 Boyer, P.D., Lardy, H. and Myrback, K. Eds. , The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 73 78. cite journal author Neuhaus FC and Byrne WL date 1959 title Metabolism of phosphoserine. II. Purification and properties of O phosphoserine phosphatase journal J. Biol. Chem. volume 234 pages 113&ndash 121 pmid 13610904 hydrolase stub Category EC 3.1.3 Category Enzymes of known structure fi Fosfoseriinifosfataasi ... more details
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