enzyme Name acetylputrescinedeacetylase EC number 3.5.1.62 CAS number 103679 48 7 IUBMB EC number 3 5 1 62 GO code 0047609 image width caption In enzymology , an acetylputrescinedeacetylase EC number 3.5.1.62 is an enzyme that catalysis catalyzes the chemical reaction N acetylputrescine H sub 2 sub O math rightleftharpoons math acetate putrescine Thus, the two substrate biochemistry substrates of this enzyme are N acetylputrescine and water H sub 2 sub O , whereas its two product chemistry products are acetate and putrescine . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N acetylputrescine acetylhydrolase . This enzyme participates in urea cycle and metabolism of amino groups . References reflist 1 cite journal author Suzuki O, Ishikawa Y, Miyazaki K, Izu, K and Matsumoto T date 1986 title Acetylputrescinedeacetylase from Micrococcus luteus K 11 journal Biochim. Biophys. Acta volume 882 pages 140&ndash 142 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
Protein deacetylase any enzyme that removes acetyl groups from lysine amino acid s in protein s. The main ones are histone deacetylase s HDACs and sirtuin s SIRT1,2,3,5 . Because histone proteins were the first known substrate for protein deacetylases the later all tend to be called HDAC s of one class or another. Human protein deacetylase enzymes have been categorized into Class I HDAC1,2,3,8 Class II HDAC4,5,6,7,9,10 , Class III SIRT1,2,3,5,6 , Class IV HDAC11 and its related enzymes . Class III are the Nicotinamide adenine dinucleotide NAD dependent protein deacetylases. References reflist Category Enzymes ... more details
enzyme Name acetylspermidine deacetylase EC number 3.5.1.48 CAS number 67339 07 5 IUBMB EC number 3 5 1 48 GO code 0047611 image width caption In enzymology , an acetylspermidine deacetylase EC number 3.5.1.48 is an enzyme that catalysis catalyzes the chemical reaction N sub 8 sub acetylspermidine H sub 2 sub O math rightleftharpoons math acetate spermidine Thus, the two substrate biochemistry substrates of this enzyme are N8 acetylspermidine and water H sub 2 sub O , whereas its two product chemistry products are acetate and spermidine . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N8 acetylspermidine amidohydrolase . Other names in common use include N8 monoacetylspermidine deacetylase , N8 acetylspermidine deacetylase , N acetylspermidine deacetylase , N1 acetylspermidine amidohydrolase incorrect , and 8 N acetylspermidine amidohydrolase . References reflist 1 cite journal author Libby PR date 1978 title Properties of an acetylspermidine deacetylase from rat liver journal Arch. Biochem. Biophys. volume 188 pages 360&ndash 3 pmid 28089 doi 10.1016 S0003 9861 78 80020 4 issue 2 cite journal author Blankenship J date 1978 title Deacetylation of N8 acetylspermidine by subcellular fractions of rat tissue journal Arch. Biochem. Biophys. volume 189 pages 20&ndash 7 pmid 708044 doi 10.1016 0003 9861 78 90109 1 issue 1 cite journal author Marchant P, Manneh VA, Blankenship J date 1986 title N1 acetylspermidine is not a substrate for N acetylspermidine deacetylase journal Biochim. Biophys. Acta. volume 881 pages 297&ndash 9 pmid 3955076 issue 2 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
enzyme Name 6 acetylglucose deacetylase EC number 3.1.1.33 CAS number 37278 46 9 IUBMB EC number 3 1 1 33 GO code 0047593 image width caption In enzymology , a 6 acetylglucose deacetylase EC number 3.1.1.33 is an enzyme that catalysis catalyzes the chemical reaction 6 acetyl D glucose H sub 2 sub O math rightleftharpoons math D glucose acetate Thus, the two substrate biochemistry substrates of this enzyme are 6 acetyl D glucose and water H sub 2 sub O , whereas its two product chemistry products are D glucose and acetate . This enzyme belongs to the family of hydrolase s, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 6 acetyl D glucose acetylhydrolase . This enzyme is also called 6 O acetylglucose deacetylase . References reflist 1 cite journal author DUFF RB, WEBLEY DM date 1958 title Metabolism of 6 O acetyl D glucopyranose and other monoacetyl sugars by strains of Bacillus megaterium and other soil organisms journal Biochem. J. volume 70 pages 520&ndash 8 pmid 13596370 issue 3 pmc 1196700 hydrolase stub Category EC 3.1.1 Category Enzymes of unknown structure ... more details
enzyme Name 4 acetamidobutyrate deacetylase EC number 3.5.1.63 CAS number 102347 82 0 IUBMB EC number 3 5 1 63 GO code 0047573 image width caption In enzymology , a 4 acetamidobutyrate deacetylase EC number 3.5.1.63 is an enzyme that catalysis catalyzes the chemical reaction 4 acetamidobutanoate H sub 2 sub O math rightleftharpoons math acetate 4 aminobutanoate Thus, the two substrate biochemistry substrates of this enzyme are 4 acetamidobutanoate and water H sub 2 sub O , whereas its two product chemistry products are acetate and 4 aminobutanoate . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4 acetamidobutanoate amidohydrolase . This enzyme participates in urea cycle and metabolism of amino groups and lysine degradation . References reflist 1 cite journal author Haywood GW and Large PJ date 1986 title 4 Acetamidobutyrate deacetylase in the yeast Candida boidinii grown on putrescine or spermidine as sole nitrogen source and its probable role in polyamine catabolism journal J. Gen. Microbiol. volume 132 pages 7&ndash 14 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
enzyme Name acetoxybutynylbithiophene deacetylase EC number 3.1.1.54 CAS number 82346 63 2 IUBMB EC number 3 1 1 54 GO code 0047373 image width caption In enzymology , an acetoxybutynylbithiophene deacetylase EC number 3.1.1.54 is an enzyme that catalysis catalyzes the chemical reaction 5 4 acetoxybut 1 ynyl 2,2 bithiophene H sub 2 sub O math rightleftharpoons math 5 4 hydroxybut 1 ynyl 2,2 bithiophene acetate Thus, the two substrate biochemistry substrates of this enzyme are 5 4 acetoxybut 1 ynyl 2,2 bithiophene and water H sub 2 sub O , whereas its two product chemistry products are 5 4 hydroxybut 1 ynyl 2,2 bithiophene and acetate . This enzyme belongs to the family of hydrolase s, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 5 4 acetoxybut 1 ynyl 2,2 bithiophene O acetylhydrolase . Other names in common use include acetoxybutynylbithiophene esterase , and 5 4 acetoxy 1 butynyl 2,2 bithiophene acetate esterase . References reflist 1 cite journal author Granander J, Sott R, Hilmersson G date 2006 title Correlation between the 6Li,15N coupling constant and the coordination number at lithium journal Chemistry. volume 12 pages 4191&ndash 7 pmid 16526078 doi 10.1002 chem.200501371 issue 15 hydrolase stub Category EC 3.1.1 Category Enzymes of unknown structure ... more details
enzyme Name chitin deacetylase EC number 3.5.1.41 CAS number 56379 60 3 IUBMB EC number 3 5 1 41 GO code 0004099 image width caption In enzymology , a chitin deacetylase EC number 3.5.1.41 is an enzyme that catalysis catalyzes the chemical reaction chitin H sub 2 sub O math rightleftharpoons math chitosan acetate Thus, the two substrate biochemistry substrates of this enzyme are chitin and water H sub 2 sub O , whereas its two product chemistry products are chitosan and acetate . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is chitin amidohydrolase . This enzyme participates in aminosugars metabolism . 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 2IW0 . References reflist 1 cite journal author Araki Y, Ito E date 1974 title A pathway of chitosan formation in Mucor rouxii enzymatic deacetylation of chitin journal Biochem. Biophys. Res. Commun. volume 56 pages 669&ndash 75 pmid 4826874 doi 10.1016 0006 291X 74 90657 3 issue 3 hydrolase stub Category EC 3.5.1 Category Enzymes of known structure tr Kitindeasetilaz ... more details
enzyme Name histone deacetylase EC number 3.5.1.98 CAS number 9076 57 7 IUBMB EC number 3 5 1 98 GO code 0046970 image 2vqj.png width caption Catalytic domain of Human HDAC4 histone deacetylase 4 with bound ... box Symbol Hist deacetyl Name Histone deacetylase superfamily image width caption Pfam PF00850 InterPro ... known as the histone deacetylase superfamily. ref name pmid9278492 cite journal author Leipe ... deacetylase inhibitors overview and perspectives journal Mol. Cancer Res. volume 5 issue 10 pages 981 ... Marks PA, Xu WS title Histone Deacetylase Inhibitors Potential in Cancer Therapy journal J. Cell ... 3 Rpd3 , which corresponds to Class I histone deacetylase 1 hda1 , corresponding to Class II and silent ... Sengupta N, Seto E title Regulation of histone deacetylase activities journal J. Cell. Biochem ... author Longworth MS, Laimins LA title Histone deacetylase 3 localizes to the plasma membrane and is a substrate ... DNA structure, preventing transcription. Histone deacetylase is involved in a series of pathways ... Deacetylase 1 journal Mol. Cell. Biol. volume 26 issue 21 pages 7913 28 year 2006 pmid 16940178 ... T, Fu C, Sakamoto KM title Role of the aggresome pathway in cancer targeting histone deacetylase ..., deacetylation of PTEN by SIRT1 deacetylase and, by HDAC1 , can stimulate its activity. ref name ... chromatin roles for HDACs. HDAC inhibitors main Histone deacetylase inhibitor Histone deacetylase ... J, Tr nkle C, Ey poglu IY, Wirth B, Bl mcke I title Histone deacetylase inhibitors possible implications ... Histone deacetylase inhibitors for epigenetic therapy of cancer journal Anticancer Drugs volume ... Histone deacetylase inhibitors as anti neoplastic agents journal Cancer Letters volume 280 issue ... Clinical development of histone deacetylase inhibitors as anticancer agents journal Annu Rev Pharmacol ... has shown that histone deacetylase inhibitors may modulate the latency of some viruses, resulting in reactivation ... 6 infection. See also Histone deacetylase inhibitor Histone methyltransferase Histone Modifying ... more details
enzyme Name acetylsalicylate deacetylase EC number 3.1.1.55 CAS number 87348 04 7 IUBMB EC number 3 1 1 55 GO code 0047610 image width caption In enzymology , an acetylsalicylate deacetylase EC number 3.1.1.55 is an enzyme that catalysis catalyzes the chemical reaction acetylsalicylate H sub 2 sub O math rightleftharpoons math salicylate acetate Thus, the two substrate biochemistry substrates of this enzyme are acetylsalicylate and water H sub 2 sub O , whereas its two product chemistry products are salicylate and acetate . This enzyme belongs to the family of hydrolase s, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is acetylsalicylate O acetylhydrolase . Other names in common use include aspirin esterase , aspirin esterase , acetylsalicylic acid esterase , and aspirin hydrolase . References reflist 1 cite journal author Ali B, Kaur S date 1983 title Mammalian tissue acetylsalicylic acid esterase s identification, distribution and discrimination from other esterases journal J. Pharmacol. Exp. Ther. volume 226 pages 589&ndash 94 pmid 6875867 issue 2 cite journal author Kim DH, Yang YS, Jakoby WB date 1990 title Aspirin hydrolyzing esterases from rat liver cytosol journal Biochem. Pharmacol. volume 40 pages 481&ndash 7 pmid 2383281 doi 10.1016 0006 2952 90 90546 W issue 3 cite journal author White KN, Hope DB date 1984 title Partial purification and characterization of a microsomal carboxylesterase specific for salicylate esters from guinea pig liver journal Biochim. Biophys. Acta. volume 785 pages 138&ndash 47 pmid 6704404 issue 3 doi 10.1016 0167 4838 84 90138 9 hydrolase stub Category EC 3.1.1 Category Enzymes of unknown structure ... more details
enzyme Name acetylornithine deacetylase EC number 3.5.1.16 CAS number 9025 12 1 IUBMB EC number 3 5 1 16 GO code 0008777 image width caption In enzymology , an acetylornithine deacetylase EC number 3.5.1.16 is an enzyme that catalysis catalyzes the chemical reaction N sub 2 sub acetyl L ornithine H sub 2 sub O math rightleftharpoons math acetate L ornithine Thus, the two substrate biochemistry substrates of this enzyme are N2 acetyl L ornithine and water H sub 2 sub O , whereas its two product chemistry products are acetate and L ornithine . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N2 acetyl L ornithine amidohydrolase . Other names in common use include acetylornithinase , N acetylornithinase , and 2 N acetyl L ornithine amidohydrolase . This enzyme participates in urea cycle and metabolism of amino groups . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2F7V and PDB link 2F8H . References reflist 1 cite journal author Vogel HJ date 1953 title Path of Ornithine Synthesis in Escherichia Coli journal Proc. Natl. Acad. Sci. U. S. A. volume 39 pages 578&ndash 83 pmid 16589307 doi 10.1073 pnas.39.7.578 issue 7 pmc 1063827 cite journal author VOGEL HJ, BONNER DM date 1956 title Acetylornithinase of Escherichia coli partial purification and some properties journal J. Biol. Chem. volume 218 pages 97&ndash 106 pmid 13278318 issue 1 hydrolase stub Category EC 3.5.1 Category Enzymes of known structure ... more details
enzyme Name N acetylgalactosaminoglycan deacetylase EC number 3.1.1.58 CAS number 52410 59 0 IUBMB EC number 3 1 1 58 GO code 0047375 image width caption In enzymology , a N acetylgalactosaminoglycan deacetylase EC number 3.1.1.58 is an enzyme that catalysis catalyzes the chemical reaction N acetyl D galactosaminoglycan H sub 2 sub O math rightleftharpoons math D galactosaminoglycan acetate Thus, the two substrate biochemistry substrates of this enzyme are N acetyl D galactosaminoglycan and water H sub 2 sub O , whereas its two product chemistry products are D galactosaminoglycan and acetate . This enzyme belongs to the family of hydrolase s, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is N acetyl D galactosaminoglycan acetylhydrolase . Other names in common use include polysaccharide deacetylase , polysaccharide deacetylase , Vi polysaccharide deacetylase , and N acetyl galactosaminoglycan deacetylase . References reflist 1 cite journal author Jorge JA, Kinney SG, Reissig JL date 1982 title Purification and characterization of Neurospora crassa N acetyl galactosaminoglycan deacetylase journal Braz. J. Med. Biol. Res. volume 15 pages 29&ndash 34 pmid 6217857 issue 1 hydrolase stub Category EC 3.1.1 Category Enzymes of unknown structure ... more details
enzyme Name 4 acetamidobutyryl CoA deacetylase EC number 3.5.1.51 CAS number IUBMB EC number 3 5 1 51 GO code 0047574 image width caption In enzymology , a 4 acetamidobutyryl CoA deacetylase EC number 3.5.1.51 is an enzyme that catalysis catalyzes the chemical reaction 4 acetamidobutanoyl CoA H sub 2 sub O math rightleftharpoons math acetate 4 aminobutanoyl CoA Thus, the two substrate biochemistry substrates of this enzyme are 4 acetamidobutanoyl CoA and water H sub 2 sub O , whereas its two product chemistry products are acetate and 4 aminobutanoyl CoA . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4 acetamidobutanoyl CoA amidohydrolase . Other names in common use include aminobutyryl CoA thiolesterase , and deacetylase thiolesterase . References reflist 1 cite journal author Ohsugi M, Kahn J, Hensley C, Chew S, Barker HA date 1981 title Metabolism of L beta lysine by a Pseudomonas. Purification and properties of a deacetylase thiolesterase utilizing 4 acetamidobutyryl CoA and related compounds journal J. Biol. Chem. volume 256 pages 7642&ndash 51 pmid 6788773 issue 14 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
enzyme Name N acetylglucosamine deacetylase EC number 3.5.1.33 CAS number 9012 32 2 IUBMB EC number 3 5 1 33 GO code 0050119 image width caption In enzymology , a N acetylglucosamine deacetylase EC number 3.5.1.33 is an enzyme that catalysis catalyzes the chemical reaction N acetyl D glucosamine H sub 2 sub O math rightleftharpoons math D glucosamine acetate Thus, the two substrate biochemistry substrates of this enzyme are N acetyl D glucosamine and water H sub 2 sub O , whereas its two product chemistry products are D glucosamine and acetate . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N acetyl D glucosamine amidohydrolase . Other names in common use include acetylaminodeoxyglucose acetylhydrolase , and N acetyl D glucosaminyl N deacetylase . This enzyme participates in aminosugars metabolism . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2C1G and PDB link 2C1I . References reflist 1 cite journal author Roseman S date 1957 title Glucosamine metabolism. I. N Acetylglucosamine deacetylase journal J. Biol. Chem. volume 226 pages 115&ndash 123 pmid 13428742 hydrolase stub Category EC 3.5.1 Category Enzymes of known structure ... more details
enzyme Name N acetylglucosamine 6 phosphate deacetylase EC number 3.5.1.25 CAS number 9027 50 3 IUBMB EC number 3 5 1 25 GO code 0008448 image width caption In enzymology , a N acetylglucosamine 6 phosphate deacetylase EC number 3.5.1.25 is an enzyme that catalysis catalyzes the chemical reaction N acetyl D glucosamine 6 phosphate H sub 2 sub O math rightleftharpoons math D glucosamine 6 phosphate acetate Thus, the two substrate biochemistry substrates of this enzyme are N acetyl D glucosamine 6 phosphate and water H sub 2 sub O , whereas its two product chemistry products are D glucosamine 6 phosphate and acetate . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N acetyl D glucosamine 6 phosphate amidohydrolase . Other names in common use include acetylglucosamine phosphate deacetylase , acetylaminodeoxyglucosephosphate acetylhydrolase , and 2 acetamido 2 deoxy D glucose 6 phosphate amidohydrolase . This enzyme participates in aminosugars 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 1O12 , PDB link 1UN7 , PDB link 1YMY , PDB link 1YRR , PDB link 2P50 , and PDB link 2P53 . References reflist 1 cite journal author White RJ, Pasternak CA date 1967 title The purification and properties of N acetylglucosamine 6 phosphate deacetylase from Escherichia coli journal Biochem. J. volume 105 pages 121&ndash 5 pmid 4861885 issue 1 pmc 1198282 cite journal doi 10.1271 bbb.60.1320 author Yamano N, Matsushita Y, Kamada Y, Fujishima S, Arita M date 1996 title Purification and characterization of N acetylglucosamine 6 phosphate deacetylase with activity against N acetylglucosamine from Vibrio cholerae non O1 journal Biosci. Biotechnol. Biochem. volume 60 pages 1320&ndash 3 pmid 8987551 issue 8 hydrolase stub Category ... more details
Infobox protein family Symbol LpxC Name UDP 3 O acyl N acetylglycosamine deacetylase image PDB 2go4 EBI.jpg width caption crystal structure of aquifex aeolicus lpxc complexed with tu 514 Pfam PF03331 Pfam clan CL0329 InterPro IPR004463 SMART PROSITE MEROPS SCOP 1nzt TCDB OPM family OPM protein CAZy CE11 CDD In molecular biology, UDP 3 O N acetylglucosamine deacetylase also known as UDP 3 O 3 hydroxymyristoyl N acetylglucosamine deacetylase or UDP 3 O acyl GlcNAc deacetylase , EC number 3.5.1. , is a bacterial enzyme involved in lipid A biosynthesis . It is a zinc dependent metallo amidase that Catalysis catalyses the second and committed step in the biosynthesis of lipid A. Lipid A anchors lipopolysaccharide the major constituent of the Bacterial outer membrane outer membrane into the membrane in Gram negative bacteria . It shows no homology to mammalia mammalian metalloamidases and is essential for cell viability , making it an important target for the development of novel antibacterial compounds. ref name pmid15667205 cite journal author Coggins BE, McClerren AL, Jiang L, Li X, Rudolph J, Hindsgaul O, Raetz CR, Zhou P title Refined solution structure of the LpxC TU 514 complex and pKa analysis of an active site histidine insights into the mechanism and inhibitor design journal Biochemistry volume 44 issue 4 pages 1114 26 year 2005 month February pmid 15667205 doi 10.1021 bi047820z url ref The secondary structure structure of UDP 3 O N acetylglucosamine deacetylase LpxC from Aquifex aeolicus has a two layer alpha beta structure similar to that of the second protein domain domain of ribosomal protein S5, only in LpxC there is a duplication giving two structural repeats of this fold, each repeat being elaborated with additional structures forming the active site . LpxC contains ..., Rusche KM, Shin H, Fierke CA, Christianson DW title Crystal structure of LpxC, a zinc dependent deacetylase ... benzoic acid derivatives synthesis and binding in the hydrophobic tunnel of the zinc deacetylase LpxC ... more details
Orphan date July 2011 enzyme Name N acetylglucosaminylphosphatidylinositol deacetylase EC number 3.5.1.89 CAS number IUBMB EC number 3 5 1 89 GO code 0000225 image width caption In enzymology , a N acetylglucosaminylphosphatidylinositol deacetylase EC number 3.5.1.89 is an enzyme that catalysis catalyzes the chemical reaction 6 N acetyl alpha D glucosaminyl 1 phosphatidyl 1D myo inositol H sub 2 sub O math rightleftharpoons math 6 alpha D glucosaminyl 1 phosphatidyl 1D myo inositol acetate Thus, the two substrate biochemistry substrates of this enzyme are 6 N acetyl alpha D glucosaminyl 1 phosphatidyl 1D myo inositol and water H sub 2 sub O , whereas its two product chemistry products are 6 alpha D glucosaminyl 1 phosphatidyl 1D myo inositol and acetate . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 6 N acetyl alpha D glucosaminyl 1 phosphatidyl 1D myo inositol acetylhydrolase . Other names in common use include N acetyl D glucosaminylphosphatidylinositol acetylhydrolase , N acetylglucosaminylphosphatidylinositol de N acetylase , GlcNAc PI de N acetylase , GlcNAc PI deacetylase , and acetylglucosaminylphosphatidylinositol deacetylase . This enzyme participates in 3 metabolism metabolic pathways glycosylphosphatidylinositol gpi anchor , , and glycan structures biosynthesis 2 . References reflist 1 cite journal author Doering TL, Masterson WJ, Englund PT, Hart GW year 1989 title Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non acetylated glucosamine journal J. Biol. Chem. volume 264 pages 11168&ndash 73 pmid 2525555 issue 19 cite journal author Kinoshita T year 1997 title Expression cloning of PIG L, a candidate N acetylglucosaminyl phosphatidylinositol deacetylase journal J. Biol. Chem. volume 272 pages 15834&ndash 40 pmid 9188481 doi 10.1074 jbc.272.25.15834 ... more details
enzyme Name cephalosporin C deacetylase EC number 3.1.1.41 CAS number 52227 71 1 IUBMB EC number 3 1 1 41 GO code 0047739 image width caption In enzymology , a cephalosporin C deacetylase EC number 3.1.1.41 is an enzyme that catalysis catalyzes the chemical reaction cephalosporin C H sub 2 sub O math rightleftharpoons math deacetylcephalosporin C acetate Thus, the two substrate biochemistry substrates of this enzyme are cephalosporin C and water H sub 2 sub O , whereas its two product chemistry products are deacetylcephalosporin C and acetate . This enzyme belongs to the family of hydrolase s, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cephalosporin C acetylhydrolase . Other names in common use include cephalosporin C acetyl hydrolase , cephalosporin C acetylase , cephalosporin acetylesterase , cephalosporin C acetylesterase , cephalosporin C acetyl esterase , and cephalosporin C deacetylase . This enzyme participates in penicillin and cephalosporin biosynthesis . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1L7A , PDB link 1ODS , PDB link 1ODT , and PDB link 1VLQ . References reflist 1 cite journal author Fujisawa Y, Shirafugi H, Kida M, Nara K, Yoneda M, Kanzaki T date 1973 title New findings on cephalosporin C biosynthesis journal Nat. New. Biol. volume 246 pages 154&ndash 5 pmid 4519146 issue 153 hydrolase stub Category EC 3.1.1 Category Enzymes of known structure ... more details
enzyme Name citrate pro 3S lyase thiolesterase EC number 3.1.2.16 CAS number 58319 93 0 IUBMB EC number 3 1 2 16 GO code 0047778 image width caption In enzymology , a citrate lyase deacetylase EC number 3.1.2.16 is an enzyme that catalysis catalyzes the chemical reaction citrate pro 3S lyase acetyl form H sub 2 sub O math rightleftharpoons math citrate pro 3S lyase thiol form acetate Thus, the two substrate biochemistry substrates of this enzyme are citrate pro 3S lyase acetyl form and water H sub 2 sub O , whereas its two product chemistry products are citrate pro 3S lyase thiol form and acetate . This enzyme belongs to the family of hydrolase s, specifically those acting on thioester bonds. The systematic name of this enzyme class is citrate pro 3S lyase acetyl form hydrolase . This enzyme is also called citrate pro 3S lyase thiolesterase . References reflist 1 cite journal author Giffhorn F, Rode H, Kuhn A, Gottschalk G date 1980 title Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation of the enzyme and studies on the inhibition by L glutamate journal Eur. J. Biochem. volume 111 pages 461&ndash 71 pmid 7460909 doi 10.1111 j.1432 1033.1980.tb04961.x issue 2 hydrolase stub Category EC 3.1.2 Category Enzymes of unknown structure ... more details
enzyme Name methylumbelliferyl acetate deacetylase EC number 3.1.1.56 CAS number 83380 83 0 IUBMB EC number 3 1 1 56 GO code 0047374 image width caption In enzymology , a methylumbelliferyl acetate deacetylase EC number 3.1.1.56 is an enzyme that catalysis catalyzes the chemical reaction 4 methylumbelliferyl acetate H sub 2 sub O math rightleftharpoons math 4 methylumbelliferone acetate Thus, the two substrate biochemistry substrates of this enzyme are 4 methylumbelliferyl acetate and water H sub 2 sub O , whereas its two product chemistry products are 4 methylumbelliferone and acetate . This enzyme belongs to the family of hydrolase s, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 4 methylumbelliferyl acetate acylhydrolase . This enzyme is also called esterase D . References reflist 1 cite journal author Hopkinson DA, Mestriner MA, Cortner J, Harris H date 1973 title Esterase D a new human polymorphism journal Ann. Hum. Genet. volume 37 pages 119&ndash 37 pmid 4768551 doi 10.1111 j.1469 1809.1973.tb01820.x issue 2 hydrolase stub Category EC 3.1.1 Category Enzymes of unknown structure ... more details
Histone deacetylase inhibitors HDAC inhibitors , HDI are a class of compounds that enzyme inhibitor interfere with the function of histone deacetylase . HDIs have a long history of use in psychiatry and neurology ..., Rifkind RA title Histone deacetylase inhibitors inducers of differentiation or apoptosis of transformed ... deacetylase inhibitors overview and perspectives journal Mol. Cancer Res. volume 5 issue 10 pages 981 9 year 2007 pmid 17951399 doi 10.1158 1541 7786.MCR 07 0324 ref The histone deacetylase inhibitors ... transcription. Histone deacetylase inhibition induces the accumulation of hyperacetylated nucleosome ... deacetylase inhibition, suppressing ligand sensitivity and regulating transcriptional activation by histone deacetylase inhibitors. Conservation of the acetylated ERalpha motif in other nuclear receptors ... functions. A number of structurally diverse histone deacetylase inhibitors have shown potent ... Histone Deacetylase Inhibition for Cancer Therapy author Vigushin D.M.1 Coombes R.C. doi 10.2174 ... of histone deacetylase inhibitors as anticancer agents journal Annu. Rev. Pharmacol. Toxicol. volume ... WD title Rational development of histone deacetylase inhibitors as anticancer agents a review journal ... author Hahnen E, Hauke J, Tr nkle C, Ey poglu IY, Wirth B, Bl mcke I title Histone deacetylase inhibitors ... author Marks PA, Dokmanovic M title Histone deacetylase inhibitors discovery and development as anticancer ... content 8 3 662.full.pdf Histone Deacetylase Inhibitors A New Class of Potential Therapeutic Agents ... Histone deacetylase inhibitors for epigenetic therapy of cancer journal Anticancer Drugs volume 18 ... . ref cite journal author Richon VM, Sandhoff TW, Rifkind RA, Marks PA title Histone deacetylase inhibitor ... T title Retinoblastoma protein recruits histone deacetylase to repress transcription journal ... journal author Matsumura T, Suzuki T, Aizawa K, et al. title The deacetylase HDAC1 negatively regulates ... title S BIO Initiates Canadian Phase 2 Clinical Trial of Oral Histone Deacetylase HDAC Inhibitor SB939 ... more details
enzyme Name N acetyldiaminopimelate deacetylase EC number 3.5.1.47 CAS number 99193 93 8 IUBMB EC number 3 5 1 47 GO code 0050118 image width caption In enzymology , a N acetyldiaminopimelate deacetylase EC number 3.5.1.47 is an enzyme that catalysis catalyzes the chemical reaction N acetyl LL 2,6 diaminoheptanedioate H sub 2 sub O math rightleftharpoons math acetate LL 2,6 diaminoheptanedioate Thus, the two substrate biochemistry substrates of this enzyme are N acetyl LL 2,6 diaminoheptanedioate and water H sub 2 sub O , whereas its two product chemistry products are acetate and LL 2,6 diaminoheptanedioate . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N6 acetyl LL 2,6 diaminoheptanedioate amidohydrolase . Other names in common use include N acetyl L diaminopimelic acid deacylase , N acetyl LL diaminopimelate deacylase , and 6 N acetyl LL 2,6 diaminoheptanedioate amidohydrolase . This enzyme participates in lysine biosynthesis . References reflist 1 cite journal author Bartlett ATM and White PJ date 1985 title Species of Bacillus that make a vegetative peptidoglycan containing lysine lack diaminopimelate epimerase but have diaminopimelate dehydrogenase journal J. Gen. Microbiol. volume 131 pages 2145&ndash 2152 cite journal author Saleh F and White PJ date 1979 title Metabolism of DD 2,6 diaminopimelic acid by a diaminopimelate requiring mutant of Bacillus megaterium journal J. Gen. Microbiol. volume 115 pages 95&ndash 100 cite journal author Sundharadas G, Gilvarg C date 1967 title Biosynthesis of alpha,epsilon diaminopimelic acid in Bacillus megaterium journal J. Biol. Chem. volume 242 pages 3983&ndash 4 pmid 4962540 issue 17 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
PBB geneid 10014 Histone deacetylase 5 is an enzyme that in humans is encoded by the HDAC5 gene . ref name pmid10220385 cite journal author Grozinger CM, Hassig CA, Schreiber SL title Three proteins define a class of human histone deacetylases related to yeast Hda1p journal Proc Natl Acad Sci U S A volume 96 issue 9 pages 4868 73 year 1999 month Jun pmid 10220385 pmc 21783 doi 10.1073 pnas.96.9.4868 ... ref name entrez Cite web title Entrez Gene HDAC5 histone deacetylase 5 url http www.ncbi.nlm.nih.gov ... II histone deacetylase acuc apha family. It possesses histone deacetylase activity and represses ... entrez Interactions Histone deacetylase 5 has been shown to Protein protein interaction interact with Zinc ... Hypertrophy through Nuclear Export of Histone Deacetylase 5 journal Mol. Cell. Biol. volume 24 issue ... May. title mHDA1 HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity .... title Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14 3 3 dependent ... quote ref See also Histone deacetylase References Reflist Further reading Refbegin 2 PBB Further reading ... deacetylase interacts with and represses MEF2A transcriptional activity journal J. Biol. Chem ... deacetylase 4 and 5 and transcriptional activity by 14 3 3 dependent cellular localization journal ... Chromosomal organization and localization of the human histone deacetylase 5 gene HDAC5 journal Biochim ... nuclear export of a histone deacetylase regulates muscle differentiation journal Nature volume ... calmodulin dependent protein kinase stimulated binding of 14 3 3 to histone deacetylase 5 journal ... pnas.260501497 pmc 18930 Cite journal author Fischle W title Human HDAC7 histone deacetylase activity ... Y title Histone deacetylase 3 associates with and represses the transcription factor GATA 2 journal ... first6 S Cite journal author Huang Y title Histone deacetylase 5 is not a p53 target gene, but its ... box yes update summary yes update citations yes DEFAULTSORT Histone Deacetylase 5 Category EC 3.5.1 ... more details
PBB geneid 3066 Histone deacetylase 2 is an enzyme that in humans is encoded by the HDAC2 gene . ref ... deacetylase 2, HDAC2 Human RPD3 , is localized to 6q21 by radiation hybrid mapping journal Genomics ... deacetylase family. Histone deacetylases act via the formation of large multiprotein complexes and are responsible .... ref name entrez cite web title Entrez Gene HDAC2 histone deacetylase 2 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 3066 accessdate ref Interactions Histone deacetylase ... is a component of a new family of histone deacetylase containing complexes journal J. Biol. Chem ... deacetylase activity journal J. Biol. Chem. volume 278 issue 43 pages 42560 8 publisher location ... histone deacetylase mediates repression of neuronal specific genes journal PNAS Proc. Natl. Acad ... of the CoREST human histone deacetylase complex journal PNAS Proc. Natl. Acad. Sci. U.S.A. volume ... RBP1 Recruits Both Histone Deacetylase Dependent and Independent Repression Activities to Retinoblastoma ... receptor gene by nuclear orphan receptors and histone deacetylase complexes journal J. Steroid ... luteinizing hormone receptor gene by histone deacetylase mSin3A complex journal J. Biol ... Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII I journal ... month Apr. title Human Sin3 deacetylase and trithorax related Set1 Ash2 histone H3 K4 methyltransferase ... year 2002 month Feb. title Isolation and characterization of a novel class II histone deacetylase ... Kook year 2002 month Oct. title Sp1 and Sp3 recruit histone deacetylase to repress transcription of human ... repressor Sp3 is associated with CK2 phosphorylated histone deacetylase 2 journal ... deacetylase complexes show enhanced catalytic activity in the presence of ATP and co immunoprecipitate .... title Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo journal J. Biol. Chem ... B Interacts with the Histone Deacetylase HDAC Corepressors HDAC1 and HDAC2 To Negatively Regulate ... more details
enzyme Name N acetyl beta alanine deacetylase EC number 3.5.1.21 CAS number 37289 04 6 IUBMB EC number 3 5 1 21 GO code 0050117 image width caption In enzymology , a N acetyl beta alanine deacetylase EC number 3.5.1.21 is an enzyme that catalysis catalyzes the chemical reaction N acetyl beta alanine H sub 2 sub O math rightleftharpoons math acetate beta alanine Thus, the two substrate biochemistry substrates of this enzyme are N acetyl beta alanine and water H sub 2 sub O , whereas its two product chemistry products are acetate and beta alanine . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N acetyl beta alanine amidohydrolase . This enzyme participates in beta alanine metabolism . References reflist 1 cite journal author Fujimoto D, Koyama T and Tamiya N date 1968 title N Acetyl beta alanine deacetylase in hog kidney journal Biochim. Biophys. Acta volume 167 pages 407&ndash 413 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
enzyme Name 5 3,4 diacetoxybut 1 ynyl 2,2 bithiophene deacetylase EC number 3.1.1.66 CAS number IUBMB EC number 3 1 1 66 GO code 0047377 image width caption In enzymology , a 5 3,4 diacetoxybut 1 ynyl 2,2 bithiophene deacetylase EC number 3.1.1.66 is an enzyme that catalysis catalyzes the chemical reaction 5 3,4 diacetoxybut 1 ynyl 2,2 bithiophene H sub 2 sub O math rightleftharpoons math 5 3 hydroxy 4 acetoxybut 1 ynyl 2,2 bithiophene acetate Thus, the two substrate biochemistry substrates of this enzyme are 5 3,4 diacetoxybut 1 ynyl 2,2 bithiophene and water H sub 2 sub O , whereas its two product chemistry products are 5 3 hydroxy 4 acetoxybut 1 ynyl 2,2 bithiophene and acetate . This enzyme belongs to the family of hydrolase s, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 5 3,4 diacetoxybut 1 ynyl 2,2 bithiophene acetylhydrolase . Other names in common use include diacetoxybutynylbithiophene acetate esterase , and 3,4 diacetoxybutinylbithiophene 4 acetate esterase . References reflist 1 cite journal author Pensl R and Suetfeld R date 1985 title Occurrence of 3,4 diacetoybutinylbithiophene in Tagetes patula and its enzymatic conversion journal Z. Naturforsch. C Biosci. volume 40 pages 3&ndash 7 hydrolase stub Category EC 3.1.1 Category Enzymes of unknown structure ... more details
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