Ligand S-adenosyl-S-carboxymethyl-L-homocysteine

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Basic Ligand Information

Molecular Structure

C₁₆H₂₂N₆O₇S

S-adenosyl-S-carboxymethyl-L-homocysteine

VFFTYSZNZJBRBG-DYXDMYNLSA-O

MetaCyc

3-thia-L-glutamate biosynthesis, 5-(methoxycarbonylmethoxy)uridine biosynthesis

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

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2.1.1.229

S-adenosyl-S-carboxymethyl-L-homocysteine + 5-methoxyuridine34 in tRNA = S-adenosyl-L-methionine + uridine 5-oxyacetic acid in tRNA

735357

Enzyme Cofactor/Cosubstrate (1 result)

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2.1.1.229

i.e. [(3S)-3-amino-3-carboxypropyl]{[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}(carboxymethyl)sulfanium, the enzyme contains a cofactor, S-adenosyl-S-carboxymethyl-L-homocysteine (SCM-SAH), in which the donor methyl group is substituted by a carboxymethyl group. The carboxyl moiety forms a salt-bridge interaction with Arg199 that is conserved in a large group of CmoA-related proteins but is not conserved in other S-adenosyl-L-methionine-containing enzymes. The active site contains one molecule cofactor S-adenosyl-S-carboxymethyl-L-homocysteine per monomer, and not S-adenosyl-L-methionine

735357