This article may be confusing or unclear to readers.(December 2022) |
pyrithiamine deaminase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.4.20 | ||||||||
CAS no. | 37289-23-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a pyrithiamine deaminase (EC 3.5.4.20) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-, methylpyridinium bromide, and H2O, whereas its 3 products are 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-, methylpyridinium bromide, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-methylpyridinium-bromide aminohydrolase.
The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the chemical reaction
The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction
Threonine ammonia-lyase (EC 4.3.1.19, systematic name L-threonine ammonia-lyase (2-oxobutanoate-forming), also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L-threonine into α-ketobutyrate and ammonia:
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In molecular biology, hydroxymethylglutaryl-CoA synthase or HMG-CoA synthase EC 2.3.3.10 is an enzyme which catalyzes the reaction in which acetyl-CoA condenses with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). This reaction comprises the second step in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA is an intermediate in both cholesterol synthesis and ketogenesis. This reaction is overactivated in patients with diabetes mellitus type 1 if left untreated, due to prolonged insulin deficiency and the exhaustion of substrates for gluconeogenesis and the TCA cycle, notably oxaloacetate. This results in shunting of excess acetyl-CoA into the ketone synthesis pathway via HMG-CoA, leading to the development of diabetic ketoacidosis.