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Deamination
Deamination
Deamination
is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver, however glutamate is also deaminated in the kidneys. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia. The rest of the amino acid is made up of mostly carbon and hydrogen, and is recycled or oxidized for energy. Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver
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Amino
In organic chemistry, amines (/əˈmiːn, ˈæmiːn/,[1][2] also UK: /ˈeɪmiːn/)[3] are compounds and functional groups that contain a basic nitrogen atom with a lone pair. Amines are formally derivatives of ammonia, wherein one or more hydrogen atoms have been replaced by a substituent such as an alkyl or aryl group[4] (these may respectively be called alkylamines and arylamines; amines in which both types of substituent are attached to one nitrogen atom may be called alkylarylamines). Important amines include amino acids, biogenic amines, trimethylamine, and aniline; see Category:Amines for a list of amines
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Thymine-DNA Glycosylase
1WYW, 2D07, 2RBA, 3UFJ, 3UO7, 3UOB, 4FNC, 4JGC, 4XEG, 4Z3A, 4Z47, 4Z7B, 4Z7Z, 5CYSIdentifiersAliases TDG, hThymine-DNA glycosylase, thymine DNA glycosylaseExternal IDs MGI: 3645587 HomoloGene: 2415 GeneCards: TDG Gene
Gene
location (Human)Chr. Chromosome
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Molecule
A molecule is an electrically neutral group of two or more atoms held together by chemical bonds.[4][5][6][7][8] Molecules are distinguished from ions by their lack of electrical charge. However, in quantum physics, organic chemistry, and biochemistry, the term molecule is often used less strictly, also being applied to polyatomic ions. In the kinetic theory of gases, the term molecule is often used for any gaseous particle regardless of its composition. According to this definition, noble gas atoms are considered molecules as they are monoatomic molecules.[9] A molecule may be homonuclear, that is, it consists of atoms of one chemical element, as with oxygen (O2); or it may be heteronuclear, a chemical compound composed of more than one element, as with water (H2O)
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DNA Methylation
DNA
DNA
methylation is a process by which methyl groups are added to the DNA
DNA
molecule. Methylation can change the activity of a DNA
DNA
segment without changing the sequence. When located in a gene promoter, DNA methylation typically acts to repress gene transcription
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AP Endonuclease
Apurinic/apyrimidinic (AP) endonuclease is an enzyme that is involved in the DNA
DNA
base excision repair pathway (BER). Its main role in the repair of damaged or mismatched nucleotides in DNA
DNA
is to create a nick in the phosphodiester backbone of the AP site
AP site
created when DNA glycosylase removes the damaged base. There are four types of AP endonucleases that have been classified according to their mechanism and site of incision. Class I AP endonucleases (EC 4.2.99.18) cleave 3' to AP sites by a β-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate
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DNA Polymerase
In molecular biology, DNA
DNA
polymerases are enzymes that synthesize DNA molecules from deoxyribonucleotides, the building blocks of DNA
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Nick Translation
Nick translation[1] (or head translation), developed in 1977 by Rigby and Paul Berg, is a tagging technique in molecular biology in which DNA Polymerase I
DNA Polymerase I
is used to replace some of the nucleotides of a DNA sequence with their labeled analogues, creating a tagged DNA
DNA
sequence which can be used as a probe in fluorescent in situ hybridization (FISH) or blotting techniques. It can also be used for radiolabeling.[2] This process is called nick translation because the DNA
DNA
to be processed is treated with DNAase to produce single-stranded "nicks". This is followed by replacement in nicked sites by DNA
DNA
polymerase I, which elongates the 3' hydroxyl terminus, removing nucleotides by 5'-3' exonuclease activity, replacing them with dNTPs
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Thymine
Thymine
Thymine
/ˈθaɪmɪn/ (T, Thy) is one of the four nucleobases in the nucleic acid of DNA
DNA
that are represented by the letters G–C–A–T. The others are adenine, guanine, and cytosine. Thymine
Thymine
is also known as 5-methyluracil, a pyrimidine nucleobase. In RNA, thymine is replaced by the nucleobase uracil. Thymine
Thymine
was first isolated in 1893 by Albrecht Kossel
Albrecht Kossel
and Albert Neumann from calves' thymus glands, hence its name.[1]Contents1 Derivation 2 Theoretical aspects 3 See also 4 References 5 External linksDerivation[edit] As its alternate name (5-methyluracil) suggests, thymine may be derived by methylation of uracil at the 5th carbon. In RNA, thymine is replaced with uracil in most cases
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Xanthine
Xanthine
Xanthine
(/ˈzænθiːn/ or /ˈzænθaɪn/; archaically xanthic acid) (3,7-dihydropurine-2,6-dione), is a purine base found in most human body tissues and fluids and in other organisms
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Uracil
Uracil
Uracil
/ˈjʊərəsɪl/ (U) is one of the four nucleobases in the nucleic acid of RNA
RNA
that are represented by the letters A, G, C and U. The others are adenine (A), cytosine (C), and guanine (G). In RNA, uracil binds to adenine via two hydrogen bonds. In DNA, the uracil nucleobase is replaced by thymine
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Adenine
Adenine
Adenine
/ˈædɪnɪn/ (A, Ade) is a nucleobase (a purine derivative). Its derivatives have a variety of roles in biochemistry including cellular respiration, in the form of both the energy-rich adenosine triphosphate (ATP) and the cofactors nicotinamide adenine dinucleotide (NAD) and flavin adenine dinucleotide (FAD). It also has functions in protein synthesis and as a chemical component of DNA
DNA
and RNA.[2] The shape of adenine is complementary to either thymine in DNA
DNA
or uracil in RNA. The adjacent image shows pure adenine, as an independent molecule. When connected into DNA, a covalent bond is formed between deoxyribose sugar and the bottom left nitrogen, so removing the hydrogen. The remaining structure is called an adenine residue, as part of a larger molecule
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APOBEC3G
2JYW, 2KBO, 2KEM, 3E1U, 3IQS, 3IR2, 3V4J, 3V4K, 4ROV, 4ROWIdentifiersAliases APOBEC3G, A3G, ARCD, ARP-9, ARP9, CEM-15, CEM15, MDS019, bK150C2.7, dJ494G10.1, apolipoprotein B m RNA
RNA
editing enzyme catalytic subunit 3GExternal IDs OMIM: 607113 HomoloGene: 128348 GeneCards: APOBEC3G Gene
Gene
ontol
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HIV
The human immunodeficiency virus (HIV) is a lentivirus (a subgroup of retrovirus) that causes HIV
HIV
infection and over time acquired immunodeficiency syndrome (AIDS).[1][2] AIDS
AIDS
is a condition in humans in which progressive failure of the immune system allows life-threatening opportunistic infections and cancers to thrive. Without treatment, average survival time after infection with HIV
HIV
is estimated to be 9 to 11 years, depending on the HIV
HIV
subtype.[3] In most cases, HIV
HIV
is a sexually transmitted infection and occurs by contact with or transfer of blood, pre-ejaculate, semen, and vaginal fluids
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AMP Deaminase
NM_001172626 NM_000036NM_001033303RefSeq (protein)NP_000027 NP_001166097NP_001028475Location (UCSC) Chr 1: 114.67 – 114.7 Mb Chr 3: 103.07 – 103.1 Mb PubMed
PubMed
search [3] [4]WikidataView/Edit Human View/Edit Mouse AMP deaminase
AMP deaminase
1 is an enzyme that in humans is encoded by the AMPD1 gene.[5][6] Adenosine monophosphate
Adenosine monophosphate
deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia molecule in the process.Contents1 Function 2 Regulation 3 Pathology 4 References 5 Further reading 6 External linksFunction[edit] Adenosine monophosphate
Adenosine monophosphate
deaminase 1 catalyzes the deamination of AMP to IMP in skeletal muscle and plays an important role in the purine nucleotide cycle
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Digital Object Identifier
In computing, a Digital Object Identifier or DOI is a persistent identifier or handle used to uniquely identify objects, standardized by the International Organization for Standardization
International Organization for Standardization
(ISO).[1] An implementation of the Handle System,[2][3] DOIs are in wide use mainly to identify academic, professional, and government information, such as journal articles, research reports and data sets, and official publications though they also have been used to identify other types of information resources, such as commercial videos. A DOI aims to be "resolvable", usually to some form of access to the information object to which the DOI refers. This is achieved by binding the DOI to metadata about the object, such as a URL, indicating where the object can be found. Thus, by being actionable and interoperable, a DOI differs from identifiers such as ISBNs and ISRCs which aim only to uniquely identify their referents
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