Sandbox Reserved 345: Difference between revisions
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=S-Adenosylmethionine decarboxylase= | =S-Adenosylmethionine decarboxylase= | ||
S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the polyamine biosynthetic pathway, forming the amine decarboxylated S-adenosylmethionine <ref name="primary">PMID: 11583147</ref><ref name="two">PMID: 9353291</ref> It also aids in the synthesis of spermine and spermidine <ref name="primary"/><ref name="three">PMID: 11583148</ref><ref name="four">PMID: 12600205</ref>. Spermine and spermidine are polyamines that are essential growth factors and critical in cell differentiation <ref name="four"/><ref name="five">PMID: 19527050</ref>. Their levels within cells are regulated by the amount of AdoMetDC available ref name="four"/>. Thus, AdoMetDC is tightly regulated in mammalian cells <ref name="primary"/>. | {{STRUCTURE_3cs9|PDB=3cs9|SCENE=Sandbox_Reserved_345/}} | ||
S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the polyamine biosynthetic pathway, forming the amine decarboxylated S-adenosylmethionine <ref name="primary">PMID: 11583147</ref><ref name="two">PMID: 9353291</ref> It also aids in the synthesis of spermine and spermidine <ref name="primary"/><ref name="three">PMID: 11583148</ref><ref name="four">PMID: 12600205</ref>. Spermine and spermidine are polyamines that are essential growth factors and critical in cell differentiation <ref name="four"/><ref name="five">PMID: 19527050</ref>. Their levels within cells are regulated by the amount of AdoMetDC available <ref name="four"/>. Thus, AdoMetDC is tightly regulated in mammalian cells <ref name="primary"/>. | |||
==Structure and Function== | ==Structure and Function== | ||
S-Adenosylmethionine decarboxylase is a (αβ)2 dimer, forming a four-layer αββα sandwich <ref name="primary"/>. The αβ monomers both have the same structure <ref name="primary"/>. The β chain consists of the residues 1-67 while the α chain contains the residues 68-329 <ref name="four"/>. Each β sheet contains eight anti-parallel β strands <ref name="primary"/>. AdoMetDC has a very unique fold compared to other large β-sandwich structures as well as other pyruvoyl-dependent amino acid decarboxylases <ref name="primary"/>. The two β sheets are connected by only one covalent bond which allows them a large amount of flexibility to behave as independently folded domains that move with respect to each other <ref name="primary"/>. The α and β subunits are formed by an internal cleavage reaction <ref name="primary"/>. | S-Adenosylmethionine decarboxylase is a (αβ)2 dimer, forming a four-layer αββα sandwich <ref name="primary"/>. The αβ monomers both have the same structure <ref name="primary"/>. The β chain consists of the residues 1-67 while the α chain contains the residues 68-329 <ref name="four"/>. Each β sheet contains eight anti-parallel β strands <ref name="primary"/>. AdoMetDC has a very unique fold compared to other large β-sandwich structures as well as other pyruvoyl-dependent amino acid decarboxylases <ref name="primary"/>. The two β sheets are connected by only one covalent bond which allows them a large amount of flexibility to behave as independently folded domains that move with respect to each other <ref name="primary"/>. The α and β subunits are formed by an internal cleavage reaction <ref name="primary"/>. | ||