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Metals/Ions
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4.3.1.17
4Fe-4S-center
the enzyme contains a [4Fe-4S]2+ cluster that acts as a Lewis acid to extract the hydroxyl group of L-serine during the dehydration reaction. Fe-S cluster binding induces protein conformational changes in L-serine dehydratase. All four iron atoms of the [4Fe-4S] cluster are coordinated with protein cysteine residues (C396, C485, C343, C385). formation of disulfide bonds between C396 and C485 and possibly between C343 and C385
747091
4.3.1.17
Ca2+
-
661725
4.3.1.17
Ca2+
may partially replace Mg2+
662950
4.3.1.17
Fe2+
iron-sulfur enzyme
651494
4.3.1.17
Fe2+
Km: 0.1 mM
210786
4.3.1.17
Fe2+
Km: 0.55 mM
210789
4.3.1.17
Fe2+
required
210786
,
210789
,
210790
4.3.1.17
Fe2+
required for activity, Fe-S cluster
650851
4.3.1.17
Fe2+
requires activation
210790
4.3.1.17
Fe2+
slight activation by FeCl2
210788
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