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Source: The Open Library
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1Biochemistry and physiology of thiamin diphosphate enzymes
By International Meeting on the Function of Thiamin Diphosphate Enzymes (1990 Blaubeuren, Germany)
“Biochemistry and physiology of thiamin diphosphate enzymes” Metadata:
- Title: ➤ Biochemistry and physiology of thiamin diphosphate enzymes
- Author: ➤ International Meeting on the Function of Thiamin Diphosphate Enzymes (1990 Blaubeuren, Germany)
- Language: English
- Number of Pages: Median: 453
- Publisher: VCH
- Publish Date: 1991
- Publish Location: Weinheim - New York
“Biochemistry and physiology of thiamin diphosphate enzymes” Subjects and Themes:
- Subjects: ➤ Congresses - Physiology - Pyruvate Dehydrogenase Complex - Pyruvate Oxidase - Thiamin pyrophosphate - Thiamin pyrophosphate-dependent enzymes - Thiamine Pyrophosphate - Transketolase - Thiamindiphosphat - Cocarboxylase - Congres - Enzym - Human physiology - Biochemistry - Enzymes
Edition Identifiers:
- The Open Library ID: OL1534065M
- Library of Congress Control Number (LCCN): 91011866
- All ISBNs: 9783527282968 - 3527282963 - 9781560811428 - 1560811420
Access and General Info:
- First Year Published: 1991
- Is Full Text Available: Yes
- Is The Book Public: No
- Access Status: Printdisabled
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Pyruvate oxidase
In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction pyruvate + phosphate + O2 ⇌ {\displaystyle \rightleftharpoons
Pyruvate dehydrogenase
proteins that possess pyruvate dehydrogenase activity include: In bacteria, a form of pyruvate dehydrogenase (also called pyruvate oxidase, EC 1.2.2.2) exists
Pyruvate oxidase (CoA-acetylating)
In enzymology, a pyruvate oxidase (CoA-acetylating) (EC 1.2.3.6) is an enzyme that catalyzes the chemical reaction pyruvate + CoA + O2 ⇌ {\displaystyle
Supramolecular catalysis
nature, pyruvate oxidase employs two cofactors thiamine pyrophosphate (ThDP) and Flavin adenine dinucleotide (FAD) to catalyze a conversion of pyruvate to
Oxidative phosphorylation
different types of ubiquinol oxidase using oxygen as an electron acceptor. Under highly aerobic conditions, the cell uses an oxidase with a low affinity for
List of EC numbers (EC 1)
aldehyde oxidase EC 1.2.3.2: Now EC 1.17.3.2, xanthine oxidase EC 1.2.3.3: pyruvate oxidase EC 1.2.3.4: oxalate oxidase EC 1.2.3.5: glyoxylate oxidase EC 1
Pyruvate dehydrogenase (quinone)
pyruvate:ubiquinone-8-oxidoreductase, pyruvate oxidase (ambiguous)) is an enzyme with systematic name pyruvate:ubiquinone oxidoreductase. This enzyme
Pyruvate dehydrogenase (cytochrome)
(cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and pyruvate oxidase (ambiguous). This enzyme participates in pyruvate metabolism. It has 2
Oxaloacetic acid
product being enol-oxaloacetate. It also arises from the condensation of pyruvate with carbonic acid, driven by the hydrolysis of ATP: CH3C(O)CO2− + HCO3−
Harmine
inhibits monoamine oxidase A (MAO-A), an enzyme which breaks down monoamines, making it a reversible inhibitor of monoamine oxidase A (RIMA). Harmine does