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Index Of Molecular Biology Articles
This is a list of topics in molecular biology. See also index of biochemistry articles. __NOTOC__ {{compact ToC, side=yes, top=yes, num=yes # 2-amino-4-deoxychorismate dehydrogenase - 2-dehydropantolactone reductase (B-specific) - 2-methylacyl-CoA dehydrogenase - 2-nitropropane dioxygenase - 2-oxobutyrate synthase - (2,3-dihydroxybenzoyl)adenylate synthase - 2,4-Dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase - 2010107G12Rik - 27-hydroxycholesterol 7alpha-monooxygenase - 3' end - 3' flanking region - 3-hydroxy-2-methylpyridinecarboxylate dioxygenase - 3-Ketosteroid 9alpha-monooxygenase - 3-oxoacyl-(acyl-carrier-protein) reductase (NADH) - (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase - 3(or 17)a-hydroxysteroid dehydrogenase - 3110001I22Rik - 3alpha-hydroxyglycyrrhetinate dehydrogenase - 4932414N04Rik - 3alpha-hydroxysteroid dehydrogenase (A-specific) - 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase - 3alpha,7alpha,12alpha-trihydroxycholestan- ...
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Molecular Biology
Molecular biology is the branch of biology that seeks to understand the molecular basis of biological activity in and between cells, including biomolecular synthesis, modification, mechanisms, and interactions. The study of chemical and physical structure of biological macromolecules is known as molecular biology. Molecular biology was first described as an approach focused on the underpinnings of biological phenomena - uncovering the structures of biological molecules as well as their interactions, and how these interactions explain observations of classical biology. In 1945 the term molecular biology was used by physicist William Astbury. In 1953 Francis Crick, James Watson, Rosalind Franklin, and colleagues, working at Medical Research Council unit, Cavendish laboratory, Cambridge (now the MRC Laboratory of Molecular Biology), made a double helix model of DNA which changed the entire research scenario. They proposed the DNA structure based on previous research done by ...
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3(or 17)a-hydroxysteroid Dehydrogenase
3(or 17)alpha-hydroxysteroid dehydrogenase (, 3(17)alpha-hydroxysteroid dehydrogenase) is an enzyme with systematic name 3(or 17)alpha-hydroxysteroid:NAD(P)+ oxidoreductase. This enzyme catalyses the chemical reaction A chemical reaction is a process that leads to the chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and break ... : androsterone + NAD(P)+ \rightleftharpoons 5alpha-androstane-3,17-dione + NAD(P)H + H+ This enzyme acts on the 3alpha-hydroxy group of androgens of the 5alpha-androstane series; and also, more slowly, on the 17alpha-hydroxy group of both androgenic and estrogenic substrates (cf. EC 1.1.1.51 3(or 17)beta-hydroxysteroid dehydrogenase). References External links * EC 1.1.1 NADH-dependent enzymes NADPH-dependent enzymes Enzymes of known structure {{1.1.1-enzyme-stub ...
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5' End
Directionality, in molecular biology and biochemistry, is the end-to-end chemical orientation of a single strand of nucleic acid. In a single strand of DNA or RNA, the chemical convention of naming carbon atoms in the nucleotide pentose-sugar-ring means that there will be a 5′ end (usually pronounced "five-prime end"), which frequently contains a phosphate group attached to the 5′ carbon of the ribose ring, and a 3′ end (usually pronounced "three-prime end"), which typically is unmodified from the ribose -OH substituent. In a DNA double helix, the strands run in opposite directions to permit base pairing between them, which is essential for replication or transcription of the encoded information. Nucleic acids can only be synthesized in vivo in the 5′-to-3′ direction, as the polymerases that assemble various types of new strands generally rely on the energy produced by breaking nucleoside triphosphate bonds to attach new nucleoside monophosphates to t ...
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4933425L06Rik
RIKEN cDNA 4933425L06 is a protein that in the house mouse is encoded by the ''4933425L06Rik'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a ba .... References Further reading * * Mouse proteins Genes mutated in mice {{Gene-stub ...
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4-Nitrophenol 4-monooxygenase
4-nitrophenol 4-monooxygenase (, ''pnpA (gene)'', ''pdcA (gene)'') is an enzyme with systematic name ''4-nitrophenol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)''. This enzyme catalyses the following chemical reaction : 4-nitrophenol + NADPH + H+ + O2 \rightleftharpoons 1,4-benzoquinone + nitrite + NADP+ + H2O 4-nitrophenol 4-monooxygenase contains FAD. References External links * {{Portal bar, Biology, border=no EC 1.14.13 ...
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4-hydroxyphenylpyruvate Oxidase
In enzymology, a 4-hydroxyphenylpyruvate oxidase () is an enzyme that catalyzes the chemical reaction :4-hydroxyphenylpyruvate + 1/2 O2 \rightleftharpoons 4-hydroxyphenylacetate + CO2 Thus, the two substrates of this enzyme are 4-hydroxyphenylpyruvate and O2, whereas its two products are 4-hydroxyphenylacetate and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating). This enzyme participates in tyrosine metabolism -Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a non-essential amino acid with a polar side group. The word "tyrosine" is from the Gr .... References * EC 1.2.3 Enzymes of unknown structure {{1.2-enzyme-stub ...
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4-hydroxyphenylacetaldehyde Oxime Monooxygenase
In enzymology, a 4-hydroxyphenylacetaldehyde oxime monooxygenase () is an enzyme that catalyzes the chemical reaction :(Z)-4-hydroxyphenylacetaldehyde oxime + NADPH + H+ + O2 \rightleftharpoons (S)-4-hydroxymandelonitrile + NADP+ + 2 H2O The 4 substrates of this enzyme are (Z)-4-hydroxyphenylacetaldehyde oxime, NADPH, H+, and O2, whereas its 3 products are (S)-4-hydroxymandelonitrile, NADP+, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (Z)-4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase. Other names in common use include 4-hydroxybenzeneacetaldehyde oxime monooxygenase, cytochrome P450II-dependent monooxygenase, NADPH-cytochrome P450 reductase (C ...
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4-Hydroxycyclohexanecarboxylate Dehydrogenase
In enzymology, a 4-hydroxycyclohexanecarboxylate dehydrogenase () is an enzyme that catalyzes Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ... the chemical reaction :trans-4-hydroxycyclohexanecarboxylate + NAD+ \rightleftharpoons 4-oxocyclohexanecarboxylate + NADH + H+ Thus, the two substrates of this enzyme are trans-4-hydroxycyclohexanecarboxylate and NAD+, whereas its 3 products are 4-oxocyclohexanecarboxylate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trans-4-hydroxycyclohexanecarboxylate:NAD+ 4-oxidoreductase. This enzyme is also called trans-4-hydroxycyclohexanecarboxylate dehydrogenase. References * ...
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4-Cresol Dehydrogenase (hydroxylating)
In enzymology, a 4-cresol dehydrogenase (hydroxylating) () is an enzyme that catalyzes the chemical reaction :4-cresol + acceptor + H2O \rightleftharpoons 4-hydroxybenzaldehyde + reduced acceptor The 3 substrates of this enzyme are 4-cresol, acceptor, and H2O, whereas its two products are 4-hydroxybenzaldehyde and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is 4-cresol:acceptor oxidoreductase (methyl-hydroxylating). Other names in common use include ''p''-cresol–(acceptor) oxidoreductase (hydroxylating), and ''p''-cresol methylhydroxylase. This enzyme participates in toluene and xylene degradation. It has 2 cofactors: FAD, and Cytochrome c. Structural studies As of late 2007, 4 structures have been solved for this class of enzymes, with PDB PDB may refer to: * Chess Problem Database Server (PDB Server) * 1,4-Dichlorobenzene (paradichlo ...
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3alpha,7alpha,12alpha-trihydroxycholestan-26-al 26-oxidoreductase
In enzymology, a 3alpha,7alpha,12alpha-trihydroxycholestan-26-al 26-oxidoreductase is an enzyme that catalysis, catalyzes the chemical reaction: :(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + NAD+ + H2O \rightleftharpoons (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + NADH + 2 H+ The 3 substrate (biochemistry), substrates of this enzyme are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al, nicotinamide adenine dinucleotide, NAD+, and water, H2O, whereas its 2 product (chemistry), products are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate, nicotinamide adenine dinucleotide, NADH, and hydrogen ion, H+. This enzyme participates in bile acid biosynthesis. Nomenclature This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The List of enzymes, systematic name of this enzyme class is (25R)-3alpha,7alpha,12alpha-trihydroxy-5be ...
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3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase
In enzymology, a 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase () is an enzyme that catalysis, catalyzes the chemical reaction :(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor \rightleftharpoons (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26- oyl-CoA + reduced acceptor The 3 substrate (biochemistry), substrates of this enzyme are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA, water, H2O, and Electron acceptor, acceptor, whereas its two product (chemistry), products are (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The List of enzymes, systematic name of this enzyme class is (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA:ac ceptor 24-oxidoreductase (24R-hydroxylating). Other names in common us ...
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3alpha-hydroxysteroid Dehydrogenase (A-specific)
In enzymology, a 3alpha-hydroxysteroid dehydrogenase (A-specific) () is an enzyme that catalyzes the chemical reaction :androsterone + NAD(P)+ \rightleftharpoons 5alpha-androstane-3,17-dione + NAD(P)H + H+ The 3 substrates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (A-specific). Structural studies As of late 2007, 11 structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made objects such as buildings and machines and natural objects such a ... have been so ...
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