"Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme". Journal of ... The term coenzyme refers specifically to enzymes and, as such, to the functional properties of a protein. On the other hand, " ... "coenzymes and cofactors". Archived from the original on 1999-08-26. Retrieved 2007-11-17. "Enzyme Cofactors". Archived from the ... Bugg T (1997). An introduction to enzyme and coenzyme chemistry. Oxford: Blackwell Science. pp. 95. ISBN 978-0-86542-793-8. ...

... enzyme.expasy.org. Retrieved 2022-11-24. Galivan JH, Allen SH (1968). "Methylmalonyl coenzyme A decarboxylase. Its role in ... This enzyme participates in propanoate metabolism. As of late 2007, two structures have been solved for this class of enzymes, ... propionyl coenzyme A carboxylase, methylmalonyl-coenzyme A decarboxylase, (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [ ... This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ...

Beinert H (1963). "Acyl coenzyme A dehydrogenase". In Boyer PD, Lardy H, Myrbäck K (eds.). The Enzymes. Vol. 7 (2nd ed.). New ... enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA ... is an enzyme with systematic name short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses ... Butyryl coenzyme A dehydrogenase". The Journal of Biological Chemistry. 206 (1): 1-12. doi:10.1016/S0021-9258(18)71290-8. PMID ...

ISBN 978-1-4899-3579-3. Q. Ashton Acton (2012). Enzymes and Coenzymes-Advances in Research and Application. ScholarlyEditions. ... Enzyme and Microbial Technology. 38 (3-4): 400-406. doi:10.1016/j.enzmictec.2005.06.013. Makhsumkhanov, A. A.; Iakubov, I. T.; ...

These are typified by the following two enzymes: Methylmalonyl coenzyme A mutase (MUT) is an isomerase enzyme which uses the ... Vitamin B12 functions as a coenzyme, meaning that its presence is required in some enzyme-catalyzed reactions. Listed here are ... Marsh EN (1999). "Coenzyme B12 (cobalamin)-dependent enzymes". Essays Biochem. 34: 139-154. doi:10.1042/bse0340139. PMID ... The vitamin activity is as a coenzyme, meaning that its presence is required for some enzyme-catalyzed reactions. ...

This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor ... The coenzyme Q : cytochrome c - oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is ... This enzyme participates in oxidative phosphorylation. It has four cofactors: cytochrome c1, cytochrome b-562, cytochrome b-566 ... It catalyzes the reduction of cytochrome c by oxidation of coenzyme Q (CoQ) and the concomitant pumping of 4 protons from the ...

Engel, Paul C.; Massey, V. (1971). "Green butyryl-coenzyme a dehydrogenase. An enzyme-acyl-coenzyme a complex". Biochemical ... Matthews, R G; Massey, V (1969). "Isolation of old yellow enzyme in free and complexed forms". J. Biol. Chem. 244 (7): 1779- ... His thesis project revolved around the enzyme fumarase (not a flavoprotein), for example a study of the effects of temperature ... Singer had recently discovered that FAD was covalently bound to the enzyme. This started Massey's career on flavins and ...

ISBN 978-0-19-850229-6. Bugg T (2004). Introduction to Enzyme and Coenzyme Chemistry. Cambridge, MA: Blackwell Publishers. ISBN ... cooperative and allosteric enzymes, interfacial and intracellular enzymes, processive enzymes and so forth. Some enzymes ... Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is ... Enzyme assays are laboratory procedures that measure the rate of enzyme reactions. Since enzymes are not consumed by the ...

Co-enzyme Q10". UK: National Institute for Health and Care Excellence. 28 March 2017. Hojerová, J (May 2000). "[Coenzyme Q10-- ... Flowers N, Hartley L, Todkill D, Stranges S, Rees K (4 December 2014). "Co-enzyme Q10 supplementation for the primary ... Coenzyme Q is a coenzyme family that is ubiquitous in animals and most bacteria (hence its other name, ubiquinone). In humans, ... Coenzyme Q10 has potential to inhibit the effects of theophylline as well as the anticoagulant warfarin; coenzyme Q10 may ...

This enzyme participates in the tricaboxylate cycle. Gergely J, Hele P, Ramakrishnan CV (1952). "Succinyl and acetyl coenzyme A ... Other names in common use include succinyl-CoA acylase, succinyl coenzyme A hydrolase, and succinyl coenzyme A deacylase. ... The enzyme succinyl-CoA hydrolase (EC 3.1.2.3) catalyzes the reaction succinyl-CoA + H2O ⇌ {\displaystyle \rightleftharpoons } ... Portal: Biology v t e (EC 3.1.2, Enzymes of unknown structure, All stub articles, EC 3.1 stubs). ...

... and catalytic enzymes which may need coenzymes (e.g. NADH, NADPH). These elements create monomers, the building blocks for ... The enzymes GOGAT and GDH catalyze the nitrogen assimilation reactions. In bacteria, the enzyme glutamate 5-kinase initiates ... Phosphate addition to UMP is catalyzed by a kinase enzyme. The enzyme CTP synthase catalyzes the next reaction step: the ... The biosynthesis of aspartate is a one step reaction that is catalyzed by a single enzyme. The enzyme aspartate ...

... a cobamide coenzyme-dependent enzyme. I Purification, assay, and properties of the enzyme". J. Biol. Chem. 243 (8): 1787-93. ... Portal: Biology v t e (EC 4.3.1, Cobamide enzymes, Enzymes of known structure, All stub articles, Enzyme stubs). ... As of early 2011, several structures have been solved for this class of enzymes. The first structure solved was the active site ... The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the chemical reaction ethanolamine ⇌ {\displaystyle \ ...

Specificities of acyl coenzyme A:phospholipid acyltransferases". J. Biol. Chem. 240: 1905-1911. PMID 14299609. Van Den Bosch H ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acyl-CoA:2-acyl-sn-glycero-3-phosphocholine O-acyltransferase. Other names in ... This enzyme participates in glycerophospholipid metabolism. Lands WE, Hart P (1965). "Metabolism of glycerolipids. VI. ...

... succinyl coenzyme A-acetoacetyl coenzyme A-transferase, and succinyl-CoA transferase. This enzyme participates in 3 metabolic ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... Menon GK, Stern JR (1960). "Enzymic synthesis and metabolism of malonyl coenzyme A and glutaryl coenzyme A". J. Biol. Chem. 235 ... As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1M3E, 1O9L, 1OOY, 1OOZ, 1OPE ...

PDC consists of other enzymes, referred to as E2 and E3. Collectively E1-E3 transform pyruvate, NAD+, coenzyme A into acetyl- ... In E. coli this enzyme is encoded by the pox B gene and the protein has a flavin cofactor. This enzyme increases the efficiency ... Thiamine enzymes, Enzymes of known structure, Autoantigens, Glycolysis). ... In terms of details, biochemical and structural data for E1 revealed a mechanism of activation of TPP coenzyme by forming the ...

Landman AD, Darkshinamurti K (March 1975). "Acetyl-Coenzyme A carboxylase. Role of the prosthetic group in enzyme ... This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme ... acetyl coenzyme A carboxylase] synthetase, acetyl coenzyme A holocarboxylase synthetase, acetyl CoA holocarboxylase synthetase ... In enzymology, a biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) is an enzyme that catalyzes the chemical reaction ATP + ...

Chistoserdova L, Vorholt JA, Thauer RK, Lidstrom ME (1998). "C1 transfer enzymes and coenzymes linking methylotrophic bacteria ...

Other names in common use include acetoacetyl coenzyme A reductase, hydroxyacyl coenzyme-A dehydrogenase, NADP+-linked ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... This enzyme participates in butanoate metabolism. Wakil S, Bressler R (March 1962). "Studies on the mechanism of fatty acid ... In enzymology, an acetoacetyl-CoA reductase (EC 1.1.1.36) is an enzyme that catalyzes the chemical reaction (R)-3-hydroxyacyl- ...

Bugg T (2012). "Chapter 10: Isomerases". Introduction to Enzyme and Coenzyme Chemistry (3rd ed.). Wiley. ISBN 978-1-118-34896-3 ... The enzyme's active site contains two Asp residues. After the substrate binds to the enzyme, the first Asp deprotonates the ... This class is further broken down by the group the enzyme acts upon: This category (EC 5.2) includes enzymes that catalyze the ... These enzymes catalyze "reactions in which a group can be regarded as eliminated from one part of a molecule, leaving a double ...

The coenzyme NAD+ is also consumed in ADP-ribose transfer reactions. For example, enzymes called ADP-ribosyltransferases add ... this can be exploited in enzyme kinetics to give information about the enzyme's mechanism. This is done by mixing an enzyme ... Despite the similarity in how proteins bind the two coenzymes, enzymes almost always show a high level of specificity for ... ISBN 978-0-7167-4339-2. Bugg T (2004). Introduction to Enzyme and Coenzyme Chemistry (2nd ed.). Blackwell Publishing Limited. ...

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups ( ... KENNEDY EP, WEISS SB (1956). "The function of cytidine coenzymes in the biosynthesis of phospholipides". J. Biol. Chem. 222 (1 ... Portal: Biology v t e (EC 2.7.7, Enzymes of unknown structure, All stub articles, EC 2.7 stubs). ... In enzymology, an ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) is an enzyme that catalyzes the chemical reaction ...

Chlorophyll production requires magnesium, while several enzymes and coenzymes require trace elements. This means, nutrient ...

Different methanogenic reactions are catalyzed by unique sets of enzymes and coenzymes. While reaction mechanism and energetics ... two coenzyme F420-dependent enzymes, from Methanosarcina barkeri". Biochimica et Biophysica Acta (BBA) - Protein Structure and ... and coenzyme F430. HS-HTP donates electrons to methyl-coenzyme M allowing the formation of methane and mixed disulfide of HS- ... The final step of H2/CO2 methanogenic involves methyl-coenzyme M reductase and two coenzymes: N-7 mercaptoheptanoylthreonine ...

The reaction carried out by these enzymes is as follows: CoA ester + H2O → free acid + coenzyme A These enzymes use the same ... "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme A. Formation of equimolar enzyme-inhibitor complex ... Acyl-coenzyme A thioesterase 4 is an enzyme that in humans is encoded by the ACOT4 gene. The protein encoded by the ACOT4 gene ... Srere PA (Dec 1965). "Palmityl-coenzyme A inhibition of the citrate-condensing enzyme". Biochimica et Biophysica Acta (BBA) - ...

The reaction carried out by these enzymes is as follows: CoA ester + H2O → free acid + coenzyme A These enzymes use the same ... "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme A. Formation of equimolar enzyme-inhibitor complex ... Acyl-coenzyme A thioesterase 11 also known as StAR-related lipid transfer protein 14 (STARD14) is an enzyme that in humans is ... Srere PA (Dec 1965). "Palmityl-coenzyme A inhibition of the citrate-condensing enzyme". Biochimica et Biophysica Acta (BBA) - ...

This enzyme is also called formyl coenzyme A hydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism. ... I. Formyl coenzyme A, an intermediate in the formate-dependent decomposition of acetyl phosphate in Clostridium kluyveri". The ... The enzyme formyl-CoA hydrolase (EC 3.1.2.10) catalyzes the reaction formyl-CoA + H2O ⇌ {\displaystyle \rightleftharpoons } CoA ... Portal: Biology v t e (EC 3.1.2, Enzymes of unknown structure, All stub articles, EC 3.1 stubs). ...

The reaction carried out by these enzymes is as follows: CoA ester + H2O → free acid + coenzyme A These enzymes use the same ... "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme A. Formation of equimolar enzyme-inhibitor complex ... It is a member of the acyl-CoA thioesterase superfamily, which is a group of enzymes that hydrolyze Coenzyme A esters. There is ... Srere PA (Dec 1965). "Palmityl-coenzyme A inhibition of the citrate-condensing enzyme". Biochimica et Biophysica Acta (BBA) - ...

The reaction carried out by these enzymes is as follows: CoA ester + H2O → free acid + coenzyme A These enzymes use the same ... "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme A. Formation of equimolar enzyme-inhibitor complex ... Acyl-CoA thioesterases, such as ACOT2, are a group of enzymes that hydrolyze Coenzyme A (CoA) esters, such as acyl-CoAs, bile ... Srere, PA (2 December 1965). "Palmityl-coenzyme A inhibition of the citrate-condensing enzyme". Biochimica et Biophysica Acta ( ...

The reaction carried out by these enzymes is as follows: CoA ester + H2O → free acid + coenzyme A These enzymes use the same ... "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme A. Formation of equimolar enzyme-inhibitor complex ... Srere PA (Dec 1965). "Palmityl-coenzyme A inhibition of the citrate-condensing enzyme". Biochimica et Biophysica Acta (BBA) - ... which catalyze the hydrolysis of various Coenzyme A esters of various molecules to the free acid plus CoA. These enzymes have ...

The reaction carried out by these enzymes is as follows: CoA ester + H2O → free acid + coenzyme A These enzymes use the same ... "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme A. Formation of equimolar enzyme-inhibitor complex ... Srere PA (Dec 1965). "Palmityl-coenzyme A inhibition of the citrate-condensing enzyme". Biochimica et Biophysica Acta (BBA) - ... which catalyze the hydrolysis of various Coenzyme A esters of various molecules to the free acid plus CoA. These enzymes have ...

... which are common to many different enzymes. For example, about 1000 enzymes are known to use the coenzyme NADH. Coenzymes are ... Enzyme levels can also be regulated by changing the rate of enzyme degradation.: 30.1.1 The opposite of enzyme induction is ... Alternatively, the enzyme can be sequestered near its substrate to activate the enzyme. For example, the enzyme can be soluble ... 8.1.1 Coenzymes are small organic molecules that can be loosely or tightly bound to an enzyme. Coenzymes transport chemical ...

"Nucleotide Co-Enzymes: A Study in Synthesis , Berkeley Graduate Lectures". gradlectures.berkeley.edu. Retrieved 27 January 2018 ... Todd, Alexander R (1949). Vitamins, coenzymes and nucleotides; a series of lectures presented at the University of Notre Dame ... and nucleotide coenzymes gained him the Nobel Prize for Chemistry in 1957. Todd was born in Cathcart in outer Glasgow, the son ...

Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D.; Lardy, H.; Myrbäck, K. (eds.). The Enzymes. Vol. 7 (2nd ed ... Medium-chain acyl-CoA dehydrogenase (EC 1.3.8.7, fatty acyl coenzyme A dehydrogenase (ambiguous), acyl coenzyme A dehydrogenase ... is an enzyme with systematic name medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme ... "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase ...

The enzyme employs one coenzyme, flavoprotein. MTRR works by catalyzing the following chemical reaction: 2 [methionine synthase ... which incorporated a coenzyme, cobalamin, also known as Vitamin B12. The coenzyme utilizes its cofactor, cobalt to catalyze the ... NADPH-dependent enzymes, Enzymes of unknown structure, All stub articles, Oxidoreductase stubs). ... This enzyme belongs to the family of oxidoreductases, to be specific those oxidizing metal ion with NAD+ or NADP+ as acceptor. ...

... malyl coenzyme A synthetase, and malate thiokinase. This enzyme participates in glyoxylate and dicarboxylate metabolism. Mue S ... This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a malate-CoA ligase (EC 6.2.1.9) is an enzyme that catalyzes the chemical reaction ATP + malate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...

Articles using infobox templates with no data rows, Coenzymes, Enzymes, Metabolism, Proteins). ... Many biotin-dependent enzymes do not contain this insertion, including all five mammalian enzymes. However, it appears the ... The connection to the rest of the enzyme at the N-terminus of BCCP core is located at the opposite end of the structure from ... However, most studies of this protein have been conducted on the E. coli form of the enzyme, where all three components exist ...