Today we are going to delve into the world of Methylenetetrahydrofolate dehydrogenase (NAD+), a topic that has been the subject of interest and debate in different areas over time. Methylenetetrahydrofolate dehydrogenase (NAD+) has aroused the curiosity and fascination of many people due to its importance in today's society. Throughout history, Methylenetetrahydrofolate dehydrogenase (NAD+) has played a fundamental role in different contexts, from politics and culture to science and technology. Throughout this article, we will explore the importance of Methylenetetrahydrofolate dehydrogenase (NAD+), as well as its impact on society at large. Additionally, we will look at how Methylenetetrahydrofolate dehydrogenase (NAD+) has evolved over time and how it has influenced our lives in ways we may not have considered before. Get ready to enter the fascinating world of Methylenetetrahydrofolate dehydrogenase (NAD+)!
methylenetetrahydrofolate dehydrogenase (NAD+) | |||||||||
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Identifiers | |||||||||
EC no. | 1.5.1.15 | ||||||||
CAS no. | 82062-90-6 | ||||||||
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 methylenetetrahydrofolate dehydrogenase (NAD+) (EC 1.5.1.15) is an enzyme that catalyzes a chemical reaction.[1]
Thus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NAD+, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NAD+ oxidoreductase. This enzyme is also called methylenetetrahydrofolate dehydrogenase (NAD+). This enzyme participates in one carbon pool by folate.[2]
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EDZ and 1EE9.[3]