Image Coenzyme M CoM .png thumb right 200px Coenzyme M Coenzyme M is a coenzyme required for methyl transfer reactions in the metabolism of methanogen s. ref cite journal author Balch WE, Wolfe RS title Specificity and biological distribution of coenzyme M 2 mercaptoethanesulfonic acid journal J. Bacteriol. volume 137 issue 1 pages 256 63 year 1979 pmid 104960 pmc 218444 ref ref cite journal author Taylor CD, Wolfe RS title Structure and methylation of coenzyme M chem HSCH 2 CH 2 SO 3 journal J. Biol. Chem. volume 249 issue 15 pages 4879 85 date 10 August 1974 pmid 4367810 url http www.jbc.org cgi reprint 249 15 4879 ref The coenzyme is an anion with the formula chem HSCH 2 CH 2 SO 3 . It is named 2 mercaptoethanesulfonate and abbreviated HS CoM. The cation is unimportant, but the mesna sodium salt is most available. Mercaptoethanesulfonate contains both a thiol , which is the main site of reactivity, and a sulfonate group, which confers solubility in aqueous media. Biochemical role The coenzyme is the C1 carrier in methanogenesis . It is converted to methyl coenzyme M, the thioether chem CH 3 SCH 2 CH 2 SO 3 , in the penultimate step to methane formation. ref cite journal doi 10.1099 00221287 144 9 2377 author Thauer RK title Biochemistry of Methanogenesis a Tribute to Marjory Stephenson journal Microbiology year 1998 volume 144 issue 9 pages 2377 2406 pmid 9782487 url http mic.sgmjournals.org cgi pmidlookup?view long&pmid 9782487 ref Coenzyme M reacts with coenzyme B , 7 thioheptanoylthreoninephosphate, to give a heterodisulfide, releasing methane chem CH 3 S CoM HS CoB &rarr chem CH 4 CoB S S CoM This conversion is catalyzed by the enzyme methyl coenzyme M reductase, which contains cofactor F430 as the prosthetic group . References reflist Enzyme cofactors Category Coenzymes Category Thiols Category Sulfonates biochem stub ca Coenzim M es Coenzima M fr Coenzyme M ja M ru zh M ... more details
File F420.png thumb Structure of Coenzyme F sub 420 sub Coenzyme F420 or 8 hydroxy 5 deazaflavin is a coenzyme involved in redox reactions in methanogen s ref cite journal author Deppenmeier U title Redox driven proton translocation in methanogenic Archaea journal Cell. Mol. Life Sci. volume 59 issue 9 pages 1513 33 year 2002 pmid 12440773 doi 10.1007 s00018 002 8526 3 ref , in many Actinobacteria , and sporadically in other bacterial lineages. It is a Flavin group flavin derivative. The coenzyme is a substrate for coenzyme F420 hydrogenase , ref cite journal author Fox JA, Livingston DJ, Orme Johnson WH, Walsh CT date 1987 title 8 Hydroxy 5 deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum 1. Purification and characterization journal Biochemistry. volume 26 pages 4219&ndash 27 pmid 3663585 doi 10.1021 bi00388a007 issue 14 ref 5,10 methylenetetrahydromethanopterin reductase and methylenetetrahydromethanopterin dehydrogenase . ref cite journal author Hagemeier CH, Shima S, Thauer RK, Bourenkov G, Bartunik HD, Ermler U title Coenzyme F420 dependent methylenetetrahydromethanopterin dehydrogenase Mtd from Methanopyrus kandleri a methanogenic enzyme with an unusual quarternary nowiki sic nowiki structure journal J. Mol. Biol. volume 332 issue 5 pages 1047 57 year 2003 pmid 14499608 doi 10.1016 S0022 2836 03 00949 5 ref ref cite journal doi 10.1016 0167 4838 91 90072 8 author GD date 1991 title Purification and properties of 5,10 methylenetetrahydromethanopterin dehydrogenase and 5,10 methylenetetrahydromethanopterin reductase, two coenzyme F420 dependent enzymes, from Methanosarcina barkeri journal Biochim. Biophys. Acta. volume 1079 pages 293&ndash 302 ... abundance of coenzyme F 420 dependent enzymes in Mycobacterium tuberculosis and other actinobacteria ... 2953692 ref . See also Coenzyme M Coenzyme B Methanofuran Tetrahydromethanopterin References reflist ... cofactors biochem stub Category Coenzymes Category Flavins de F420 fr Coenzyme F420 ja F420 ru ... more details
chembox Watchedfields changed verifiedrevid 425859719 ImageFile Coenzyme B CoB .svg ImageSize IUPACName 2 7 mercapto 1 oxoheptyl amino 3 phosphonooxybutanoic acid OtherNames Section1 Chembox Identifiers InChI 1 C11H22NO7PS c1 8 19 20 16,17 18 10 11 14 15 12 9 13 6 4 2 3 5 7 21 h8,10,21H,2 7H2,1H3, H,12,13 H,14,15 H2,16,17,18 t8 ,10 m1 s1 InChIKey JBJSVEVEEGOEBZ PSASIEDQBT InChI1 1 C11H22NO7PS c1 8 19 20 16,17 18 10 11 14 15 12 9 13 6 4 2 3 5 7 21 h8,10,21H,2 7H2,1H3, H,12,13 H,14,15 H2,16,17,18 InChIKey1 JBJSVEVEEGOEBZ UHFFFAOYAG SMILES1 O C NC C O O C OP O O O C CCCCCCS StdInChI Ref stdinchicite correct chemspider StdInChI 1S C11H22NO7PS c1 8 19 20 16,17 18 10 11 14 15 12 9 13 6 4 2 3 5 7 21 h8,10,21H,2 7H2,1H3, H,12,13 H,14,15 H2,16,17,18 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey JBJSVEVEEGOEBZ UHFFFAOYSA N CASNo Ref cascite correct ?? CASNo 104302 77 4 PubChem 350 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 343 SMILES O C N C H C O O C H OP O O O C CCCCCCS Section2 Chembox Properties Formula chem C 11 H 22 NO 7 PS MolarMass 343.333641 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Coenzyme B is a coenzyme required for redox reactions in methanogen s. The full chemical name of coenzyme B is 7 mercaptoheptanoylthreoninephosphate. ref cite journal author Noll KM, Rinehart KL, Tanner RS, Wolfe RS title Structure of component B 7 mercaptoheptanoylthreonine phosphate of the methylcoenzyme ... ref The molecule contains a thiol , which is its principal site of reaction. Coenzyme B reacts with 2 methylthioethanesulfonate methyl Coenzyme M , abbreviated chem CH 3 S CoM , to release methane ...?view long&pmid 9782487 doi 10.1099 00221287 144 9 2377 ref chem link coenzyme M CH 3 S CoM HS CoB &rarr chem CH 4 CoB S S CoM This conversion is catalyzed by the enzyme methyl coenzyme M reductase ... fr Coenzyme B gl Coencima B ja B ru B ... more details
DISPLAYTITLE Coenzyme Q sub 10 sub chembox verifiedrevid 477001960 ImageFile Ubiquinone.png IUPACName ... br Quinone br Plastoquinone Coenzyme Q sub 10 sub , also known as ubiquinone , ubidecarenone , coenzyme ... Coenzyme Q oxidation reduction reactions in mitochondrial electron transport pages 65 82 title Coenzyme ... 122 4 year 1994 pmid 8288904 ref There are three redox states of coenzyme Q sub 10 sub fully oxidized ... Coenzyme Q sub 10 sub was first discovered by Professor Fredrick L. Crane and colleagues at the University ... The oxidized structure of CoQ sub 10 sub is shown on the top right. The various kinds of Coenzyme ... common Coenzyme Q in human mitochondria is CoQ sub 10 sub . Q refers to the quinone head and 10 ... http www.mbschachter.com coenzyme q10.htm ref CoQ sub 10 sub inhibits lipid peroxidation by preventing ... of Coenzyme Q in Eukaryotes journal Mitochondrion volume 7 issue Suppl pages S62 71 year 2007 month ... of synthesis in animal cells. ref cite journal author Bentinger M, Tekle M, Dallner G title Coenzyme ... cite journal last1 Bhagavan first1 Hemmi N. last2 Chopra first2 Raj K. title Coenzyme Q sub 10 ... in intestinal coenzyme Q sub 10 sub absorption by food intake journal Yakugaku Zasshi volume 127 issue ... be noted that CoQ sub 9 sub is the predominant form of coenzyme Q in rats. ref cite book ... T. last5 Okamoto first6 T. last6 Kishi chapter Metabolism and Exogenous Coenzyme Q sub 10 sub in vivo and Bioavailability of Coenzyme Q sub 10 sub Preparations in Japan title Biomedical and Clinical Aspects of Coenzyme Q pages 131 42 publisher Elsevier location Amsterdam year 1964 ref It appears that CoQ ... Trevisson E, Dimauro S, Navas P, Salviati L title Coenzyme Q deficiency in muscle journal Curr. Opin .... title Safety and tolerability of high dosage coenzyme Q sub 10 sub in Huntington s disease and healthy .... ref cite journal author Hathcock JN, Shao A title Risk assessment for coenzyme Q sub 10 sub Ubiquinone ... author Montero R, S nchez Alc zar JA, Briones P, et al. title Analysis of coenzyme Q sub 10 sub in muscle ... more details
Infobox disease Name Coenzyme Q10 deficiency Image Ubiquinone.png Alt Caption Ubiquinone DiseasesDB ICD10 ICD9 ICDO OMIM 607426 MedlinePlus eMedicineSubj eMedicineTopic MeshID Coenzyme Q10 deficiency is a deficiency of Coenzyme Q10 . It can be associated with COQ2 , APTX , PDSS2 , PDSS1 , CABC1 , and COQ9 . ref OMIM 607426 ref Some forms may be more treatable than other mitochondrial disease s. ref name pmid19375058 cite journal author Duncan AJ, Bitner Glindzicz M, Meunier B, et al. title A nonsense mutation in COQ9 causes autosomal recessive neonatal onset primary coenzyme Q10 deficiency a potentially treatable form of mitochondrial disease journal Am. J. Hum. Genet. volume 84 issue 5 pages 558 66 year 2009 month May pmid 19375058 pmc 2681001 doi 10.1016 j.ajhg.2009.03.018 url http linkinghub.elsevier.com retrieve pii S0002 9297 09 00115 3 ref References reflist Disorders of TCA and ETC Mitochondrial diseases Category Mitochondrial diseases Category TCA and ETC metabolism disorders disease stub ... more details
enzyme Name coenzyme F420 hydrogenase EC number 1.12.98.1 CAS number 9027 05 8 IUBMB EC number 1 12 98 1 GO code 0050454 image width caption In enzymology , a coenzyme F420 hydrogenase EC number 1.12.98.1 is an enzyme that catalysis catalyzes the chemical reaction H sub 2 sub coenzyme F sub 420 sub math rightleftharpoons math reduced coenzyme F sub 420 sub Thus, the two substrate biochemistry substrates of this enzyme are hydrogen H sub 2 sub and coenzyme F420 , whereas its product chemistry product is reduced coenzyme F420. This enzyme belongs to the family of oxidoreductase s, specifically those acting on hydrogen as donor with other, known, acceptors. The systematic name of this enzyme class is hydrogen coenzyme F420 oxidoreductase . Other names in common use include 8 hydroxy 5 deazaflavin reducing hydrogenase , F420 reducing hydrogenase , and coenzyme F420 dependent hydrogenase . This enzyme participates in folate biosynthesis and is a critical part of energy conservation in some methanogens such as Methanosarcina barkeri . It has 3 cofactor biochemistry cofactors iron , nickel , and deazaflavin . References reflist 1 cite journal author Adams MWW, Mortenson LE and Chen J S date 1981 title Hydrogenase journal Biochim. Biophys. Acta volume 594 pages 105&ndash 176 cite journal author Yamazaki S date 1982 title A selenium containing hydrogenase from Methanococcus vannielii Identification of the selenium moiety as a selenocysteine residue journal J. Biol. Chem. volume 257 pages 7926&ndash 9 pmid 6211447 issue 14 cite journal author Fox JA, Livingston DJ, Orme Johnson WH, Walsh CT date 1987 title 8 Hydroxy 5 deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum 1. Purification and characterization journal Biochemistry. volume 26 pages 4219&ndash 27 pmid 3663585 doi 10.1021 bi00388a007 issue 14 cite journal author Muth E, Morschel E, Klein A date 1987 ... title Purification and properties of the membrane associated coenzyme F420 reducing hydrogenase from ... more details
Infobox Disease Name 3 hydroxyacyl coenzyme A dehydrogenase deficiency Image Caption DiseasesDB 34396 ICD10 ICD9 ICDO OMIM 601609 OMIM mult OMIM2 231530 MedlinePlus eMedicineSubj eMedicineTopic MeshID 3 hydroxyacyl coenzyme A dehydrogenase deficiency HADH deficiency is a rare condition that prevents the body from converting certain fats to energy, particularly during fasting. Normally, through a process called fatty acid oxidation , several enzymes work in a step wise fashion to metabolize fats and convert them to energy. People with 3 hydroxyacyl coenzyme A dehydrogenase deficiency have inadequate levels of an enzyme required for a step that metabolizes groups of fats called medium chain fatty acid s and short chain fatty acid s for this reason this disorder is sometimes called medium and short chain 3 hydroxyacyl coenzyme A dehydrogenase M SCHAD deficiency. Typically, initial signs and symptoms of this disorder occur during infancy or early childhood and can include poor appetite, vomiting, diarrhea, lethargy , hypoglycemia , hypotonia , liver problems, and abnormally high levels of hyperinsulinism . Insulin controls the amount of sugar that moves from the blood into cells for conversion to energy. Individuals with 3 hydroxyacyl coenzyme A dehydrogenase deficiency are also at risk for complications such as seizures, life threatening heart and breathing problems, coma, and sudden unexpected death. Problems related to 3 hydroxyacyl coenzyme A dehydrogenase deficiency can be triggered by periods of fasting or by illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome , a severe disorder that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated ... levels of an enzyme called 3 hydroxyacyl coenzyme A dehydrogenase . Medium chain and short chain ... Genetics Home Reference 3 hydroxyacyl coenzyme A dehydrogenase deficiency Fatty acid metabolism disorders ... more details
enzyme Name coenzyme B sulfoethylthiotransferase EC number 2.8.4.1 CAS number IUBMB EC number 2 8 4 1 GO code 0050524 image width caption In enzymology , coenzyme B sulfoethylthiotransferase , also known as methyl coenzyme M reductase MCR or most systematically as 2 methylthio ethanesulfonate N 7 thioheptanoyl 3 O phosphothreonine S 2 sulfoethyl thiotransferase is an enzyme that catalysis catalyzes the final step in the formation of methane . It does so by combining the hydrogen donor coenzyme B and the methyl donor coenzyme M . Via this enzyme, most of the natural gas on earth was produced. Ruminant s e.g. cows produce methane because their rumens contain methanogen methanogenic prokaryotes Archaea ref http microbewiki.kenyon.edu index.php Bovine Rumen Methanogens ref ref pmid 11384509 ref that encode and express the set of genes of this enzymatic complex. The enzyme has two active site s, each occupied by the nickel containing Cofactor F430 F sub 430 sub Cofactor biochemistry cofactor . ref http mic.sgmjournals.org cgi content abstract 144 9 2377?maxtoshow &hits 10&RESULTFORMAT &searchid 1&FIRSTINDEX 0&sortspec relevance&volume 144&firstpage 2377&resourcetype HWCIT Thauer, R. K., Biochemistry of methanogenesis a tribute to Marjory Stephenson , Microbiology, 1998, 144, 2377 2406. DOI 10.1099 00221287 144 9 2377 PMID 9782487 ref 2 methylthio ethanesulfonate methyl CoM N 7 mercaptoheptanoyl threonine 3 O phosphate coenzyme B math rightleftharpoons math CoM S S CoB methane Thus, the two substrate biochemistry substrates of this enzyme are 2 methylthio ethanesulfonate and N 7 mercaptoheptanoyl ... in folate biosynthesis . Citation needed date February 2012 Structure coenzyme B sulfoethylthiotransferase ... of coenzyme M and 7 mercaptoheptanoylthreonine phosphate is a product of the methylreductase ... with highly purified methyl coenzyme M reductase component C from Methanobacterium thermoautotrophicum ... Category Anaerobic digestion enzyme stub fr M thyl coenzyme M r ductase ... more details
No footnotes date March 2011 Infobox Disease Name Isobutyryl coenzyme A dehydrogenase deficiency Image L valine skeletal.svg Caption Valine DiseasesDB 34225 ICD10 ICD9 ICDO OMIM 604773 MedlinePlus eMedicineSubj eMedicineTopic MeshID Isobutyryl coenzyme A dehydrogenase deficiency , commonly known as IBD deficiency , is a rare metabolic disorder in which the body is unable to process certain amino acid s properly. People with this disorder have inadequate levels of an enzyme that helps break down the amino acid valine , resulting in a build up of valine in the urine, a symptom called valinuria . Diagnosis Babies with this disorder are usually healthy at birth. The signs and symptoms may not appear until later in infancy or childhood and can include poor feeding and growth failure to thrive , a weakened and enlarged heart dilated cardiomyopathy , seizures, and low numbers of red blood cells anemia . Another feature of this disorder may be very low blood levels of carnitine a natural substance that helps convert certain foods into energy . Isobutyryl CoA dehydrogenase deficiency may be worsened by long periods without food fasting or infections that increase the body s demand for energy. Some individuals with gene mutations that can cause isobutyryl CoA dehydrogenase deficiency may never experience any signs and symptoms of the disorder. Genetics Image autorecessive.svg thumb right Isobutyryl coenzyme A dehydrogenase deficiency has an autosomal recessive pattern of inheritance. Defects in the ACAD8 gene cause isobutyryl coenzyme A dehydrogenase deficiency. The ACAD8 gene provides instructions for making an enzyme that plays an essential role in breaking down proteins from the diet. Specifically, the enzyme is responsible for processing valine, an amino acid that is part of many proteins. If a mutation in the ACAD8 gene reduces or eliminates the activity of this enzyme, the body ... coenzyme A External links NLM isobutyrylcoenzymeadehydrogenasedeficiency Amino acid metabolic ... more details
PBB geneid 3033 Hydroxyacyl Coenzyme A dehydrogenase also known as HADH is an enzyme which in humans is encoded by the HADH gene . ref name pmid975867 cite journal author Craig I, Tolley E, Bobrow M title A preliminary analysis of the segregation of human hydroxyacyl coenzyme A dehydrogenase in human mouse somatic cell hybrids journal Cytogenet. Cell Genet. volume 16 issue 1 5 pages 114 7 year 1976 pmid 975867 doi 10.1159 000130568 url ref ref name pmid16176262 cite journal author Yang SY, He XY, Schulz H title 3 Hydroxyacyl CoA dehydrogenase and short chain 3 hydroxyacyl CoA dehydrogenase in human health and disease journal FEBS J. volume 272 issue 19 pages 4874 83 year 2005 month October pmid 16176262 doi 10.1111 j.1742 4658.2005.04911.x url ref Function This gene is a member of the 3 hydroxyacyl CoA dehydrogenase gene family. The encoded protein functions in the mitochondrial matrix to catalyze the oxidation of straight chain 3 hydroxyacyl CoAs as part of the beta oxidation pathway. Its enzymatic activity is highest with medium chain length fatty acids. ref name entrez cite web title Entrez Gene HADH url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 3033 accessdate ref Clinical significance Mutations in this gene cause one form of familial hyperinsulinemic hypoglycemia . ref name pmid14693719 cite journal author Molven A, Matre GE, Duran M, Wanders RJ, Rishaug U, Nj lstad PR, Jellum E, S vik O title Familial hyperinsulinemic hypoglycemia caused by a defect in the SCHAD enzyme of mitochondrial fatty acid oxidation journal Diabetes volume 53 issue 1 pages 221 7 year 2004 month January pmid 14693719 doi 10.2337 diabetes.53.1.221 url http diabetes.diabetesjournals.org cgi pmidlookup?view long&pmid 14693719 ref A deficiency is associated with 3 hydroxyacyl coenzyme A dehydrogenase deficiency . See also 3 hydroxyacyl CoA dehydrogenase References Reflist External links http www.ncbi.nlm.nih.gov books NBK1375 GeneReviews NCBI NIH UW entry ... more details
Voet which is depicted in the image below. The first step involves displacement of coenzyme A CoA from ... Residues Crystal structures for the E. coli SCS provide evidence that the coenzyme A molecular ... dehydrogenase and succinyl coenzyme A synthetase roles of ArcA, Fnr, and the upstream sdhCDAB ... subunit of succinate coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial ... External links MeshName Succinyl Coenzyme A Synthetases Ligases Citric acid cycle enzymes Mitochondrial ... more details
No footnotes date September 2011 Infobox disease Name Medium chain acyl coenzyme A dehydrogenase deficiency MCAD ICD10 ICD9 ICD9 277.85 ICDO Image Caption OMIM 201450 MedlinePlus eMedicineSubj ped eMedicineTopic 1392 DiseasesDB Medium chain acyl coenzyme A dehydrogenase deficiency MCADD is a fatty acid oxidation disorder associated with inborn error of metabolism inborn errors of metabolism . It is due to defects in the enzyme complex known as medium chain acyl dehydrogenase MCAD and reduced activity of this complex. This complex oxidizes medium chain fatty acids fatty acids having 6 10 carbons while reducing FAD to FADH sub 2 sub . citation needed date March 2012 It is recognized as one of the more rare causes of sudden infant death syndrome SIDS , although it may be better described as a mimic, rather than a cause, of SIDS. Citation needed date January 2008 Overview Two main types of fat ... down in stages by the successive removal of molecules of acetyl coenzyme A, which contains 2 carbon ... to coenzyme A , a series of four reactions, each catalyzed by a different enzyme, is required to remove each acetyl coenzyme A molecule. As the first step involves removal of hydrogen atoms i.e. ... with these various proteins are Very long chain acyl coenzyme A dehydrogenase deficiency VLCAD deficiency Long chain 3 hydroxyacyl coenzyme A dehydrogenase deficiency LCHAD deficiency Medium chain acyl coenzyme A dehydrogenase deficiency MCAD deficiency Short chain acyl coenzyme A dehydrogenase deficiency SCAD deficiency 3 hydroxyacyl coenzyme A dehydrogenase deficiency M SCHAD deficiency Diagnosis ... thumb right Medium chain acyl coenzyme A dehydrogenase deficiency has an Recessive gene autosomal ... chain acyl coenzyme A dehydrogenase enzyme. This condition is inherited in an recessive gene ... br.fcgi?book gene&part mcad GeneReview NIH UW entry on Medium Chain Acyl Coenzyme A Dehydrogenase Deficiency GPnotebook 422903871 Fatty acid metabolism disorders DEFAULTSORT Medium Chain Acyl Coenzyme ... more details
No footnotes date September 2011 Infobox disease Name Long chain 3 hydroxyacyl coenzyme A dehydrogenase deficiency ICD10 ICD9 ICD9 277.85 ICDO Image Caption OMIM 600890 MedlinePlus eMedicineSubj ped eMedicineTopic 1284 DiseasesDB Long chain 3 hydroxyacyl coenzyme A dehydrogenase deficiency , often shortened to LCHAD deficiency , is a rare autosomal recessive fatty acid oxidation disorder that prevents the body from converting certain lipid fat s into energy. This can become life threatening, particularly during periods of fasting . Image LCHAD deficiency.jpg right thumb 200px Schematic demonstrating mitochondria l fatty acid beta oxidation and effects of LCHAD deficiency Genetics Image autorecessive.svg thumb right Long chain 3 hydroxyacyl coenzyme A dehydrogenase deficiency has an autosomal recessive pattern of inheritance. Mutation s in the HADHA gene lead to inadequate levels of an enzyme called long chain 3 hydroxyacyl coenzyme A CoA dehydrogenase, which is part of a protein complex known as mitochondrial trifunctional protein . Long chain fatty acid s from food and body fat cannot be Fatty acid metabolism metabolized and processed without sufficient levels of this enzyme . As a result, these fatty acids are not converted to energy, which can lead to characteristic features of this disorder, such as lethargy and hypoglycemia . Long chain fatty acids or partially metabolized fatty acids may build up in tissues and damage the liver , heart , retina , and muscles, causing more serious complications. Symptoms Typically, initial signs and symptoms of this disorder occur during infancy or early childhood and can include feeding difficulties, lethargy , hypoglycemia , hypotonia , liver problems, and abnormalities in the retina . Muscle pain, a breakdown of muscle tissue, and abnormalities in the nervous system that affect arms and legs peripheral neuropathy may occur later ... disorders DEFAULTSORT Long Chain 3 Hydroxyacyl Coenzyme A Dehydrogenase Deficiency Category Fatty acid ... more details
refimprove date August 2010 Infobox disease Name Short chain acyl coenzyme A dehydrogenase deficiency ICD10 ICD9 ICD9 277.85 ICDO Image Caption OMIM 201470 MedlinePlus eMedicineSubj eMedicineTopic DiseasesDB 31599 Short chain acyl coenzyme A dehydrogenase deficiency SCADD , also called ACADS deficiency and SCAD deficiency , ref name omim OMIM 201470 ref is an autosome autosomal dominance genetics recessive ref name scadar cite pmid 18977676 ref List of fatty acid metabolism disorders fatty acid oxidation disorder which affects enzymes required to break down a certain group of fats called short chain fatty acid s. Characteristics Some affected infants will exhibit vomiting, low blood sugar hypoglycemia , a lack of energy lethargy , poor feeding, and failure to gain weight and grow at the expected rate failure to thrive . Other features of this disorder may include poor muscle tone hypotonia , seizures, developmental delays, and a small head size microcephaly . The symptoms of short chain acyl CoA dehydrogenase deficiency may be triggered by periods of fasting or during illnesses such as viral infections. In some cases, signs and symptoms may not appear until adulthood, when some individuals may develop muscle weakness and wasting. Other people with gene mutations that can cause this disorder may have such mild symptoms that they are never diagnosed. Many biochemical geneticists consider this to be a biochemical phenotype with a very mild clinical phenotype or no clinical phenotype. Cause and Genetics Image Autorecessive.jpg thumb right Short chain acyl coenzyme A dehydrogenase deficiency has an autosomal recessive pattern of inheritance. SCADD is caused by mutation s in the ACADS gene, located on chromosome chromosome 12 human 12q22 qter . ref name pmid18054510 cite journal ... data get data.php?hgnc id HGNC 90 ACADS gene RareDiseases 4822 Short chain acyl coenzyme A CoA ...?view long&pmid 14595061 Fatty acid metabolism disorders DEFAULTSORT Short Chain Acyl Coenzyme A Dehydrogenase ... more details
ferricytochrome c oxidoreductase . Other names in common use include coenzyme Q cytochrome c reductase ... oxidoreductase, reduced coenzyme Q cytochrome c reductase, ubiquinone cytochrome c oxidoreductase, reduced ... cytochrome c oxidoreductase, coenzyme QH2 cytochrome c reductase, and QH2 cytochrome c oxidoreductase ... c by oxidation of coenzyme Q CoQ and the concomitant pumping of 4 protons from the mitochondrial ... thumb 400px The Q cycle The reaction mechanism for complex III Cytochrome bc1, Coenzyme Q Cytochrome ... complexes in membranes MeshName Coenzyme Q Cytochrome c Reductase Diphenol family oxidoreductases ... Coenzima Q citocromo c reductasa fr Coenzyme Q cytochrome c r ductase id Koenzim Q sitokrom c reduktase ... more details
unreferenced date January 2008 Infobox disease Name Very long chain acyl coenzyme A dehydrogenase deficiency ICD10 ICD9 ICD9 277.85 ICDO Image Caption OMIM 201475 MedlinePlus eMedicineSubj eMedicineTopic DiseasesDB Very long chain acyl coenzyme A dehydrogenase deficiency VLCADD is a fatty acid oxidation disorder which prevents the body from converting certain fats to energy, particularly during periods without food. Those affected by this disorder have inadequate levels of an enzyme that breaks down a group of fats called very long chain fatty acids. Diagnosis Typically, initial signs and symptoms of this disorder occur during infancy and include low blood sugar hypoglycemia , lack of energy lethargy , and muscle weakness. There is also a high risk of complications such as liver abnormalities and life threatening heart problems. Symptoms that begin later in childhood, adolescence, or adulthood tend to be milder and usually do not involve heart problems. Episodes of very long chain acyl coenzyme A dehydrogenase deficiency can be triggered by periods of fasting, illness, and exercise. It is common for babies and children with the early and childhood types of VLCADD to have episodes of illness called metabolic crises. Some of the first symptoms of a metabolic crisis are extreme sleepiness, behavior changes, irritable mood, poor appetite. Some of these other symptoms of VLCADD in infants may also follow fever , nausea , diarrhea , vomiting , hypoglycemia . Treatment If a metabolic crisis is not treated, a child with VLCADD can develop breathing problems, seizures, coma , sometimes leading to death. Genetics Image autorecessive.svg thumb right Very long chain acyl coenzyme A dehydrogenase ... lead to inadequate levels of an enzyme called very long chain acyl coenzyme A CoA dehydrogenase. Without ... coenzyme A dehydrogenase deficiency NLM verylongchainacylcoenzymeadehydrogenasedeficiency http www.newbornscreening.info ... in Genetics STAR G Project Fatty acid metabolism disorders DEFAULTSORT Very Long Chain Acyl Coenzyme ... more details
F420 may refer to Coenzyme F420 , a coenzyme involved in redox reactions in methanogens HMNZS Tutira F420 , a 1948 Loch class frigate of the Royal New Zealand Navy Letter NumberCombDisambig ... more details
protein Name hydroxyacyl Coenzyme A dehydrogenase 3 ketoacyl Coenzyme A thiolase enoyl Coenzyme A hydratase trifunctional protein , alpha subunit caption image width HGNCid 4801 Symbol HADHA AltSymbols EntrezGene 3030 OMIM 600890 RefSeq NM 000182 UniProt P40939 PDB ECnumber 1.1.1.211 Chromosome 2 Arm p Band 23 LocusSupplementaryData HADHA is a gene associated with long chain 3 hydroxyacyl coenzyme A dehydrogenase deficiency . See also Mitochondrial trifunctional protein biochem stub Multienzyme complexes Lipid metabolism enzymes ... more details
chembox verifiedrevid 277881712 ImageFile Octanoyl coenzyme A.svg ImageSize 300px IUPACName OtherNames Section1 Chembox Identifiers CASNo 1264 52 4 PubChem 380 SMILES MeSHName octanoyl coenzyme A Section2 Chembox Properties Formula C sub 29 sub H sub 50 sub N sub 7 sub O sub 17 sub P sub 3 sub S MolarMass 893.732 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Octanoyl coenzyme A is the endpoint of beta oxidation in peroxisome s. biochemistry stub Category Coenzymes fa fr Octanoyl coenzyme A ... more details
Lead too short date September 2009 chembox verifiedrevid 319493451 ImageFile Isovaleryl coenzyme A.svg ImageSize 300px IUPACName OtherNames Section1 Chembox Identifiers CASNo 6244 91 3 PubChem 810 SMILES MeSHName isovaleryl coenzyme A Section2 Chembox Properties Formula C sub 26 sub H sub 44 sub N sub 7 sub O sub 17 sub P sub 3 sub S MolarMass 851.652 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Isovaleryl coenzyme A is an intermediate in branched chain amino acids metabolism. See also Isovaleryl coenzyme A dehydrogenase Amino acid metabolism intermediates References Reflist DEFAULTSORT Isovaleryl Coa Category Coenzymes biochem stub fa fr Isoval ryl coenzyme A ja CoA ... more details
enzyme Name hydroxymethylglutaryl CoA hydrolase EC number 3.1.2.5 CAS number 9025 89 2 IUBMB EC number 3 1 2 5 GO code 0047994 image width caption In enzymology , a hydroxymethylglutaryl CoA hydrolase EC number 3.1.2.5 is an enzyme that catalysis catalyzes the chemical reaction S 3 hydroxy 3 methylglutaryl CoA H sub 2 sub O math rightleftharpoons math CoA 3 hydroxy 3 methylglutarate Thus, the two substrate biochemistry substrates of this enzyme are S 3 hydroxy 3 methylglutaryl CoA and water H sub 2 sub O , whereas its two product chemistry products are coenzyme A CoA and 3 hydroxy 3 methylglutarate. This enzyme belongs to the family of hydrolase s, specifically those acting on thioester bonds. The systematic name of this enzyme class is S 3 hydroxy 3 methylglutaryl CoA hydrolase. Other names in common use include beta hydroxy beta methylglutaryl coenzyme A hydrolase, beta hydroxy beta methylglutaryl coenzyme A deacylase, hydroxymethylglutaryl coenzyme A hydrolase, hydroxymethylglutaryl coenzyme A deacylase, and 3 hydroxy 3 methylglutaryl CoA hydrolase. References reflist 1 cite journal author DEKKER EE, SCHLESINGER MJ, COON MJ date 1958 title beta Hydroxy beta methylglutaryl coenzyme A deacylase journal J. Biol. Chem. volume 233 pages 434&ndash 8 pmid 13563516 issue 2 hydrolase stub Category EC 3.1.2 Category Enzymes of unknown structure ... more details
chembox verifiedrevid 265862835 ImageFile Isobutyryl coenzyme A.png ImageSize 250px IUPACName small S 2 3 nowiki nowiki 4 nowiki nowiki 5 6 Aminopurin 9 yl 4 hydroxy 3 phosphonooxyoxolan 2 yl methoxy hydroxyphosphoryl oxy hydroxyphosphoryl oxy 2 hydroxy 3,3 dimethylbutanoyl amino propanoylamino ethyl 2 methylpropanethioate small OtherNames Isobutyryl coenzyme A Section1 Chembox Identifiers CASNo 15621 60 0 PubChem 808 SMILES CC C C O SCCNC O CCNC O C C C C COP O O OP O O OCC1C C C O1 N2C NC3 C2N CN C3N O OP O O O O MeSHName Isobutyryl coenzyme A Section2 Chembox Properties Formula C sub 25 sub H sub 42 sub N sub 7 sub O sub 17 sub P sub 3 sub S MolarMass 837.62 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Isobutyryl coenzyme A is an intermediate in the metabolism of valine . See also Isobutyryl CoA mutase Isobutyryl coenzyme A dehydrogenase deficiency Amino acid metabolism intermediates Category Coenzymes organic compound stub fa fr Isobutyryl coenzyme A ja CoA ... more details
Unreferenced date December 2009 Protein Name acyl Coenzyme A dehydrogenase, long chain caption image width HGNCid 88 Symbol ACADL AltSymbols EntrezGene 33 OMIM 609576 RefSeq NM 001608 UniProt P28330 PDB ECnumber 1.3.99.3 Chromosome 2 Arm q Band 34 LocusSupplementaryData q35 ACADL is a gene associated with long chain 3 hydroxyacyl coenzyme A dehydrogenase deficiency . See also Acyl CoA dehydrogenase Lipid metabolism enzymes DEFAULTSORT Acadl Biochem stub es ACADL ... more details
enzyme Name glutathione CoA glutathione transhydrogenase EC number 1.8.4.3 CAS number 37256 48 7 IUBMB EC number 1 8 4 3 GO code 0047140 image width caption In enzymology , a glutathione CoA glutathione transhydrogenase EC number 1.8.4.3 is an enzyme that catalysis catalyzes the chemical reaction CoA glutathione disulfide math rightleftharpoons math CoA glutathione glutathione Thus, the two substrate biochemistry substrates of this enzyme are coenzyme A CoA and glutathione disulfide , whereas its two product chemistry products are CoA glutathione and glutathione . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is CoA glutathione disulfide oxidoreductase . Other names in common use include glutathione coenzyme A glutathione disulfide transhydrogenase , glutathione coenzyme A glutathione disulfide transhydrogenase , glutathione coenzyme A glutathione transhydrogenase , glutathione coenzyme A glutathione transhydrogenase , coenzyme A oxidized glutathione oxidoreductase , and coenzyme A glutathione disulfide oxidoreductase . This enzyme participates in cysteine metabolism and glutathione metabolism . References reflist 1 cite journal author Chang SH, Wilken DR date 1966 title Participation of the unsymmetrical disulfide of coenzyme A and glutathione in an enzymatic sulfhydryl disulfide interchange. I Partial purification and properties of the bovine kidney enzyme journal J. Biol. Chem. volume 241 pages 4251&ndash 60 pmid 5924646 issue 18 1.8 enzyme stub Category EC 1.8.4 Category Enzymes of unknown structure it Glutatione CoA glutatione transidrogenasi ja CoA ... more details
enzyme Name 4 Coumarate CoA ligase EC number 6.2.1.12 CAS number 37332 51 7 IUBMB EC number 6 2 1 12 GO code 0016207 image width caption In enzymology , a 4 coumarate CoA ligase EC number 6.2.1.12 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 coumarate CoA math rightleftharpoons math AMP diphosphate 4 coumaroyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 4 coumarate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 4 coumaroyl CoA . This enzyme belongs to the family of ligase s, to be specific those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 4 coumarate CoA ligase AMP forming . Other names in common use include 4 coumaroyl CoA synthetase , p coumaroyl CoA ligase , p coumaryl coenzyme A synthetase , p coumaryl CoA synthetase , p coumaryl CoA ligase , feruloyl CoA ligase , hydroxycinnamoyl CoA synthetase , 4 coumarate coenzyme A ligase , caffeolyl coenzyme A synthetase , p hydroxycinnamoyl coenzyme A synthetase , feruloyl coenzyme A synthetase , sinapoyl coenzyme A synthetase , 4 coumaryl CoA synthetase , hydroxycinnamate CoA ligase , p coumaryl CoA ligase , p hydroxycinnamic acid CoA ligase , and 4CL . This enzyme participates in phenylpropanoid biosynthesis . References reflist 1 cite journal author Gross GG, Zenk MH date 1974 title Isolation and properties of hydroxycinnamate CoA ligase from lignifying tissue of Forsythia journal Eur. J. Biochem. volume 42 pages 453 9 pmid 4364250 doi 10.1111 j.1432 1033.1974.tb03359.x issue 2 cite journal author Lindl T, Kreuzaler F, Hahlbrock K date 1973 title Synthesis of p coumaroyl coenzyme a with a partially purified p coumarate CoA ligase from cell suspension cultures of soybean Glycine max journal Biochim. Biophys. Acta. volume 302 pages 457 64 pmid 4699252 issue 2 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure fr 4 coum ... more details
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