CHEBI:85535 - N-succinyl-L-α-amino acid(2−)

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ChEBI Name N-succinyl-L-α-amino acid(2−) ChEBI ID CHEBI:85535 ChEBI ASCII Name N-succinyl-L-alpha-amino acid(2-) Definition A doubly-charged N-acyl-L-α-amino acid anion resulting from deprotonation of both carboxy groups of N-succinyl-L-α-amino acid. Major species at pH 7.3. Stars This entity has been manually annotated by the ChEBI Team. Submitter Gemma Holliday Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C6H6NO5R Net Charge -2 Average Mass (excl. R groups) 172.116 Monoisotopic Mass (excl. R groups) 172.02460 SMILES C[C@H](NC(=O)CCC([O-])=O)C([O-])=O ChEBI Ontology Outgoing N-succinyl-L-α-amino acid(2−) (CHEBI:85535) is a N-acyl-L-α-amino acid anion (CHEBI:59874) N-succinyl-L-α-amino acid(2−) (CHEBI:85535) is a dicarboxylic acid dianion (CHEBI:28965) N-succinyl-L-α-amino acid(2−) (CHEBI:85535) is conjugate base of N-succinyl-L-α-amino acid (CHEBI:191191) Incoming N-succinyl-L-α-amino acid (CHEBI:191191) is conjugate acid of N-succinyl-L-α-amino acid(2−) (CHEBI:85535) Synonym Source N-succinyl-L-α-amino acid dianion ChEBI Citation Sakai A, Xiang DF, Xu C, Song L, Yew WS, Raushel FM, Gerlt JA (2006) Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway for the irreversible conversion of D- to L-amino acids. Biochemistry 45, 4455-4462 (Source: SUBMITTER) [PubMed:16584181] [show Abstract] Members of the mechanistically diverse enolase superfamily catalyze reactions that are initiated by abstraction of the alpha-proton of a carboxylate anion to generate an enolate anion intermediate that is stabilized by coordination to a Mg2+ ion. The catalytic groups, ligands for an essential Mg2+ and acid/base catalysts, are located in the (beta/alpha)8-barrel domain of the bidomain proteins. The assigned physiological functions in the muconate lactonizing enzyme (MLE) subgroup (Lys acid/base catalysts at the ends of the second and sixth beta-strands in the barrel domain) are cycloisomerization (MLE), dehydration (o-succinylbenzoate synthase; OSBS), and epimerization (L-Ala-D/L-Glu epimerase). We previously studied a putatively promiscuous member of the MLE subgroup with uncertain physiological function from Amycolatopsis that was discovered based on its ability to catalyze the racemization of N-acylamino acids (N-acylamino acid racemase; NAAAR) but also catalyzes the OSBS reaction [OSBS/NAAAR; Palmer, D. R., Garrett, J. B., Sharma, V., Meganathan, R., Babbitt, P. C., and Gerlt, J. A. (1999) Biochemistry 38, 4252-4258]. In this manuscript, we report functional characterization of a homologue of this protein encoded by the genome of Geobacillus kaustophilus as well as two other proteins that are encoded by the same operon, a divergent member of the Gcn5-related N-acetyltransferase (GNAT) superfamily of enzymes whose members catalyze the transfer an acyl group from an acyl-CoA donor to an amine acceptor, and a member of the M20 peptidase/carboxypeptidase G2 family. We determined that the member of the GNAT superfamily is succinyl-CoA:D-amino acid N-succinyltransferase, the member of the enolase superfamily is N-succinylamino acid racemase (NSAR), and the member of the M20 peptidase/carboxypeptidase G2 family is N-succinyl-L-amino acid hydrolase. We conclude that (1) these enzymes constitute a novel, irreversible pathway for the conversion of D- to L-amino acids and (2) the NSAR reaction is a new physiological function in the MLE subgroup. The NSAR is also functionally promiscuous and catalyzes an efficient OSBS reaction; intriguingly, the operon for menaquinone biosynthesis in G. kaustophilus does not encode an OSBS, raising the possibility that the NSAR is a bifunctional enzyme rather than an accidentally promiscuous enzyme. Last Modified 20 April 2022