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 [1][2] It also aids in the synthesis of spermine and spermidine [1][3][4]. Spermine and spermidine are polyamines that are essential growth factors and critical in cell differentiation [4][5]. Their levels within cells are regulated by the amount of AdoMetDC available [4]. Thus, AdoMetDC is tightly regulated in mammalian cells [1]. | S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the polyamine biosynthetic pathway, forming the amine decarboxylated S-adenosylmethionine [1][2] It also aids in the synthesis of spermine and spermidine [1][3][4]. Spermine and spermidine are polyamines that are essential growth factors and critical in cell differentiation [4][5]. Their levels within cells are regulated by the amount of AdoMetDC available [4]. Thus, AdoMetDC is tightly regulated in mammalian cells [1]. | ||
{{ | {{STRUCTURE_3cs9|PDB=3cs9|SCENE=Sandbox_Reserved_345/Begining/1}} | ||
==Structure and Function== | ==Structure and Function== | ||
S-Adenosylmethionine decarboxylase is a (αβ)2 dimer, forming a four-layer αββα sandwich [1]. The αβ monomers both have the same structure [1]. The β chain consists of the residues 1-67 while the α chain contains the residues 68-329 [4]. Each β sheet contains eight anti-parallel β strands [1]. AdoMetDC has a very unique fold compared to other large β-sandwich structures as well as other pyruvoyl-dependent amino acid decarboxylases [1]. 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 [1]. The α and β subunits are formed by an internal cleavage reaction [1]. | S-Adenosylmethionine decarboxylase is a (αβ)2 dimer, forming a four-layer αββα sandwich [1]. The αβ monomers both have the same structure [1]. The β chain consists of the residues 1-67 while the α chain contains the residues 68-329 [4]. Each β sheet contains eight anti-parallel β strands [1]. AdoMetDC has a very unique fold compared to other large β-sandwich structures as well as other pyruvoyl-dependent amino acid decarboxylases [1]. 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 [1]. The α and β subunits are formed by an internal cleavage reaction [1]. | ||