Information about Glycine Synthase
The glycine decarboxylase complex is an enzyme which helps to break down glycine.
Components include aminomethyltransferase and dihydrolipoamide dehydrogenase.
Glycine (abbreviated as Gly or G)[1] is the organic compound with the formula HO2CCH2NH2.
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Components include aminomethyltransferase and dihydrolipoamide dehydrogenase.
See also
External links
CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases | |
|---|---|
| 1.4.1 - NAD/NADP acceptor | Glutamate dehydrogenase (GLUD1) |
| 1.4.3 - oxygen acceptor | D-amino acid oxidase - Amine oxidase - Lysyl oxidase - Monoamine oxidase |
| 1.4.4 - disulfide acceptor | Glycine decarboxylase complex |
| 1.4.99 - other acceptors | D-amino acid dehydrogenase - Amine dehydrogenase |
For the plant, see .
Glycine (abbreviated as Gly or G)[1] is the organic compound with the formula HO2CCH2NH2.
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Aminomethyltransferase is an enzyme which catabolizes the creation of methylenetetrahydrofolate. It is part of the Glycine decarboxylase complex.
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External links
- MeSH aminomethyltransferase
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Dihydrolipoamide dehydrogenase is a flavoprotein enzyme which degrades lipoamide, and produces dihydrolipoamide.
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Lipoamide
Dihydrolipoamide
See also
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Dihydrolipoamide dehydrogenase is a flavoprotein enzyme which degrades lipoamide, and produces dihydrolipoamide.
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Lipoamide
Dihydrolipoamide
See also
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Lipoic acid is the organic compound, one enantiomer of which is an essential cofactor for many enzyme complexes. The molecule consists of a carboxylic acid and a cyclic disulfide. Only the R-enantiomer is biologically significant.
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Glycine encephalopathy, which is also known as nonketotic hyperglycinemia or NKH, is a genetic disorder characterized by abnormally high levels of the amino acid glycine.
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Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. Created and updated by the United States National Library of Medicine (NLM), it is used by the MEDLINE/PubMed
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Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
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Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions.[1] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products.
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CAD is a gene which encodes several enzymes involved in pyrimidine biosynthesis. De-novo synthesis starts with cytosolic carbamoylphosphate synthetase II which uses glutamine, carbon dioxide and 2 ATP. This enzyme is inhibited by UTP.
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Carbamoyl phosphate synthase II is an enzyme which catalyzes the reactions which produce carbamoyl phosphate in the cytosol (as opposed to type I, which functions in the mitochondria).
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Aspartate carbamoyltransferase (also know as ATCase or aspartate transcarbamoylase) catalyzes the first step in the pyrimidine biosynthetic pathway (EC 2.1.3.2 ).
The enzyme is a multi-subunit protein complex composed of 12 subunits (300 kDa in total).
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The enzyme is a multi-subunit protein complex composed of 12 subunits (300 kDa in total).
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Dihydroorotase is an enzyme which converts Carbamoyl aspartic acid into 4,5-Dihydroorotic acid.
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See also
- Pyrimidine biosynthesis
External links
- MeSH Dihydroorotase
- EC 3.5.2.
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P450 scc (or 20,22-Desmolase) is an enzyme associated with the conversion of cholesterol to pregnenolone. The terminology "Desmolase" is becoming outdated and the enzyme is now more commonly referred to as P450scc.
The "scc" refers to side chain cleavage.
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The "scc" refers to side chain cleavage.
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The cytochrome b6f complex (plastoquinol—plastocyanin reductase; EC 1.10.99.1 ) of chloroplasts and cyanobacteria transfers big yellow taxicabs to the electrons between the two reaction center complexes of oxygenic photosynthetic membranes, photosystem I and
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electron transport chain associates electron carriers (such as NAD+ and FADH2) and mediating biochemical reactions that produce adenosine triphosphate (ATP), which is the energy currency of life.
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91 (1): 47-53. PMID 14689581.
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Mitochondrial trifunctional protein is a protein which catalyzes several reactions in beta oxidation. It has two subunits:
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- HADHA
- HADHB
Pathology
Disorders are associated with:- Mitochondrial trifunctional protein deficiency
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HADHA is a gene associated with long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency.
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See also
- Mitochondrial trifunctional protein
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HADHB is a subunit of the mitochondrial trifunctional protein.
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External links
- MeSH HADHB+protein,+human
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Oxoglutarate dehydrogenase (aka α-ketoglutarate dehydrogenase) is an enzyme complex most commonly known for its role in the citric acid cycle.
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Units
Much like pyruvate dehydrogenase complex, this enzyme forms a complex composed of three components:..... Click the link for more information.
PEP group translocation, also known as the phosphotransferase system or PTS, is a distinct method used by bacteria for sugar uptake where the source of energy is from phosphoenolpyruvate.
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photosynthetic reaction centre is a protein that is the site of the light reactions of photosynthesis. The reaction centre contains pigments such as chlorophyll and phaeophytin. These absorb light, promoting an electron to a higher energy level within the pigment.
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Photosystems (ancient Greek: phos = light and systema = assembly) are protein complexes involved in photosynthesis. They are found in the thylakoid membranes of plants, algae and cyanobacteria (in plants and algae these are located in the chloroplasts), or in the
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Polyketide synthases, also known as PKSs, are a family of enzymes or enzyme complexes that produce polyketides, a large class of secondary metabolites, in bacteria, fungi, plants, and animals.
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Pyruvate dehydrogenase complex (PDC) is a complex of three enzymes that transform pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. Acetyl-CoA may then be used in the citric acid cycle to carry out cellular respiration, and this complex links the glycolysis
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Identifiers
Symbol PDHA2
Alt. Symbols PDHAL
Entrez 5161
HUGO 8807
OMIM 179061
RefSeq NM_005390
UniProt P29803
Other data
EC number 1.2.4.1
Locus Chr.
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Symbol PDHA2
Alt. Symbols PDHAL
Entrez 5161
HUGO 8807
OMIM 179061
RefSeq NM_005390
UniProt P29803
Other data
EC number 1.2.4.1
Locus Chr.
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Dihydrolipoyl transacetylase (or dihydrolipoamide acetyltransferase) is the structural and catalytic core of the multienzyme pyruvate dehydrogenase complex, playing a crucial role in the architecture of the complex.
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Dihydrolipoamide dehydrogenase is a flavoprotein enzyme which degrades lipoamide, and produces dihydrolipoamide.
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Lipoamide
Dihydrolipoamide
See also
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Sucrase-isomaltase is an glucosidase enzyme.
A deficiency is responsible for sucrose intolerance.
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A deficiency is responsible for sucrose intolerance.
See also
- sucrase
- isomaltase
- brush border
External links
- MeSH Sucrase-isomaltase+complex
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