9J0U

Crystal structure of monomeric PLP-dependent transaminase from Desulfobacula toluolica in F 41 3 2 space group

This is a non-PDB format compatible entry.

Summary for 9J0U

• Entry DOI: 10.2210/pdb9j0u/pdb
• Descriptor: Dat: predicted D-alanine aminotransferase (2 entities in total)
• Functional Keywords: daat, d-amino acid transaminase, plp, ta, monomeric ta, transferase
• Biological source: Desulfobacula toluolica
• Total number of polymer chains: 1
• Total formula weight: 32285.30

Authors

Matyuta, I.O.,Bakunova, A.K.,Nikolaeva, A.Y.,Rakitina, T.V.,Bezsudnova, E.Y.,Popov, V.O.,Boyko, K.M. (deposition date: 2024-08-03, release date: 2024-09-18, Last modification date: 2025-01-22)

Primary citation

Bakunova, A.K.,Matyuta, I.O.,Nikolaeva, A.Y.,Rakitina, T.V.,Boyko, K.M.,Popov, V.O.,Bezsudnova, E.Y.
From Structure to Function: Analysis of the First Monomeric Pyridoxal-5'-Phosphate-Dependent Transaminase from the Bacterium Desulfobacula toluolica .
Biomolecules, 14:-, 2024

PubMed Abstract: The first monomeric pyridoxal-5'-phosphate (PLP)-dependent transaminase from a marine, aromatic-compound-degrading, sulfate-reducing bacterium Tol2, has been studied using structural, kinetic, and spectral methods. The monomeric organization of the transaminase was confirmed by both gel filtration and crystallography. The PLP-dependent transaminase is of the fold type IV and deaminates D-alanine and ()-phenylethylamine in half-reactions. The enzyme shows high stereoselectivity; no deamination of L-amino acids and ()-phenylethylamine is detected. Structural analysis and subsequent mutagenesis led to the conclusion that the monomeric architecture of the enzyme is the only one possible and sufficient for stereoselectivity and PLP binding, but not for the overall double-substrate transamination reaction and the stability of the holo form with the reduced cofactor-pyridoxamine-5'-phosphate. These results extend the structural university of the PLP fold type IV enzymes and demonstrate the need for deeper analysis of the sequence-structure-function relationships in the transaminases.

PubMed: 39766298
DOI: 10.3390/biom14121591

Experimental method

X-RAY DIFFRACTION (2.58 Å)