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Literature summary for 5.1.1.3 extracted from

  • Liechti, G.; Singh, R.; Rossi, P.; Gray, M.; Adams, N.; Maurelli, A.
    Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase and diaminopimelate epimerase activities (2018), mBio, 9, pii: e00204-18 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene dapF, sequence comparisons and phylogenetic analysis, Chlamydia trachomatis dapF restores growth in an Escherichia coli D-glutamate auxotroph strain WM335 laos lacking endogenaous gene dapF, expression under the control of an arabinose-inducible promoter, the recombinant enzyme is capable of both DAP epimerase and D-glut racemase activities, DapFCT is also capable of racemizing D-Glu to L-Glu Chlamydia trachomatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate Chlamydia trachomatis
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D-glutamate
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r
additional information Chlamydia trachomatis Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase and diaminopimelate epimerase, EC 5.1.1.7, activities. Diaminopimelate and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the PLP cofactor ?
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?

Organism

Organism UniProt Comment Textmining
Chlamydia trachomatis
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
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Chlamydia trachomatis D-glutamate
-
r
additional information Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase and diaminopimelate epimerase, EC 5.1.1.7, activities. Diaminopimelate and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the PLP cofactor Chlamydia trachomatis ?
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?

Synonyms

Synonyms Comment Organism
D-glutamate racemase
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Chlamydia trachomatis
DapF
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Chlamydia trachomatis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate the glutamate racemase activity is dependent on the cofactor pyridoxal phosphate Chlamydia trachomatis

General Information

General Information Comment Organism
evolution a large number of Chlamydia species (as well as members of the Planctomycetes-Verrucomicrobiae-Chlamydiae superphylum) possess DapF but lack homologues of MurI. It is likely that DapF is a primordial isomerase that functions as both racemase and epimerase in these organisms, suggesting that specialized D-glutamate racemase enzymes never evolved in these microbes. DapFCT possesses an additional cysteine (C86) that is not highly conserved in other bacterial species Chlamydia trachomatis
metabolism D-glutamate is generated via the racemization of L-glutamate by glutamate racemase (MurI). Chlamydia lacks homologues of MurI. The bifunctional diaminopimelate epimerase (DapF) also synthesizes D-glutamate, EC 5.1.1.3, and catalyzes the final step in the synthesis of meso-diaminopimelate, an amino acid unique to peptidoglycan, EC 5.1.1.7 Chlamydia trachomatis
additional information the structure of Chlamydia DAP epimerase exhibits significant remodeling in the substrate-binding pocket, overview. DapFCT requires the epimerase active-site cysteines for glutamate racemase activity Chlamydia trachomatis
physiological function DapF is a primordial isomerase that functions as both racemase and epimerase in the organism. genetic complementation of an Escherichia coli murI mutant demonstrating that Chlamydia DapF can generate D-glutamate. D-Glu racemase activity is required for synthesizing D-Glu-containing peptidoglycan, DapFCT is also capable of racemizing D-Glu to L-Glu Chlamydia trachomatis