Analysis of catalytic determinants of diaminopimelate and ornithine decarboxylases using alternate substrates

Fogle, Emily J.; Toney, Michael D.

doi:10.1016/j.bbapap.2011.05.014

Cited by 13 publications

(19 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…From a functional point of view, there is evidence that diaminopimelate decarboxylase and d -ornithine/ d -lysine decarboxylase have a concerted decarboxylation/protonation step, ruling out the quinonoid intermediate formation (Fogle and Toney 2011 ; Phillips et al 2019 ). This could explain the lack of O 2 reactivity.…”

Section: A Structural Basis For Oxygen Reactivity Of Decarboxylasesmentioning

confidence: 99%

Oxygen reactivity with pyridoxal 5′-phosphate enzymes: biochemical implications and functional relevance

et al. 2020

View full text Add to dashboard Cite

The versatility of reactions catalyzed by pyridoxal 5′-phosphate (PLP) enzymes is largely due to the chemistry of their extraordinary catalyst. PLP is necessary for many reactions involving amino acids. Reaction specificity is controlled by the orientation of the external aldimine intermediate that is formed upon addition of the amino acidic substrate to the coenzyme. The breakage of a specific bond of the external aldimine gives rise to a carbanionic intermediate. From this point, the different reaction pathways diverge leading to multiple activities: transamination, decarboxylation, racemization, elimination, and synthesis. A significant novelty appeared approximately 30 years ago when it was reported that some PLP-dependent decarboxylases are able to consume molecular oxygen transforming an amino acid into a carbonyl compound. These side paracatalytic reactions could be particularly relevant for human health, also considering that some of these enzymes are responsible for the synthesis of important neurotransmitters such as γ-aminobutyric acid, dopamine, and serotonin, whose dysregulation under oxidative conditions could have important implications in neurodegenerative states. However, the reactivity of PLP enzymes with dioxygen is not confined to mammals/animals. In fact, some plant PLP decarboxylases have been reported to catalyze oxidative reactions producing carbonyl compounds. Moreover, other recent reports revealed the existence of new oxidase activities catalyzed by new PLP enzymes, MppP, RohP, Ind4, CcbF, PvdN, Cap15, and CuaB. These PLP enzymes belong to the bacterial and fungal kingdoms and are present in organisms synthesizing bioactive compounds. These new PLP activities are not paracatalytic and could only scratch the surface on a wider and unexpected catalytic capability of PLP enzymes.

show abstract

Section: A Structural Basis For Oxygen Reactivity Of Decarboxylasesmentioning

confidence: 99%

Oxygen reactivity with pyridoxal 5′-phosphate enzymes: biochemical implications and functional relevance

et al. 2020

View full text Add to dashboard Cite

show abstract

“…A 200 µL reaction mixture containing 20 m M O ‐phospho‐ l ‐serine, 10 m M α‐ketoglutarate, 100 m M NaCl, 50 m M pH 7.3 HEPES, and either 10 µ M EUBREC_2651 or no enzyme (negative control) was allowed to react for 2.5 h at which point the protein was denatured with 2 µL glacial acetic acid and the precipitated protein was removed by centrifugation. The reaction mixture was derivatized with o‐ phthalaldehyde (OPA) and analyzed by HPLC as previously described …”

Section: Methodsmentioning

confidence: 99%

“…The reaction mixture was derivatized with o-phthalaldehyde (OPA) and analyzed by HPLC as previously described. 86…”

Section: Hplc Detection Of Eubrec_2651 Reaction Productsmentioning

confidence: 99%

Molecular characterization of novel pyridoxal‐5′‐phosphate‐dependent enzymes from the human microbiome

et al. 2014

Self Cite

View full text Add to dashboard Cite

Pyridoxal-5 0 -phosphate or PLP, the active form of vitamin B6, is a highly versatile cofactor that participates in a large number of mechanistically diverse enzymatic reactions in basic metabolism. PLP-dependent enzymes account for~1.5% of most prokaryotic genomes and are estimated to be involved in~4% of all catalytic reactions, making this an important class of enzymes. Here, we structurally and functionally characterize three novel PLP-dependent enzymes from bacteria in the human microbiome: two are from Eubacterium rectale, a dominant, nonpathogenic, fecal, Gram-positive bacteria, and the third is from Porphyromonas gingivalis, which plays a major role in human periodontal disease. All adopt the Type I PLP-dependent enzyme fold and

show abstract

“…However, the activation mechanism of Fe 2+ on decarboxylase was still unclear. For the PLP-dependent decarboxylation, it referred to the transfer of the proton during the elimination of the CO 2 [27]. Fe 2+ has been reported to be a good metal as redox center, which might be associated with its role in the activation of lysine decarboxylase [28].…”

Section: Discussionmentioning

confidence: 99%

Efficient Production of Enantiopure d-Lysine from l-Lysine by a Two-Enzyme Cascade System

Wang

Cao

et al. 2016

Catalysts

View full text Add to dashboard Cite

Abstract:The microbial production of D-lysine has been of great interest as a medicinal raw material. Here, a two-step process for D-lysine production from L-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase was developed. The whole-cell activities of engineered Escherichia coli expressing racemases from the strains Proteus mirabilis (LYR) and Lactobacillus paracasei (AAR) were first investigated comparatively. When the strain BL21-LYR with higher racemization activity was employed, L-lysine was rapidly racemized to give DL-lysine, and the D-lysine yield was approximately 48% after 0.5 h. Next, L-lysine was selectively catabolized to generate cadaverine by lysine decarboxylase. The comparative analysis of the decarboxylation activities of resting whole cells, permeabilized cells, and crude enzyme revealed that the crude enzyme was the best biocatalyst for enantiopure D-lysine production. The reaction temperature, pH, metal ion additive, and pyridoxal 5 -phosphate content of this two-step production process were subsequently optimized. Under optimal conditions, 750.7 mmol/L D-lysine was finally obtained from 1710 mmol/L L-lysine after 1 h of racemization reaction and 0.5 h of decarboxylation reaction. D-lysine yield could reach 48.8% with enantiomeric excess (ee) ≥ 99%.

show abstract

Analysis of catalytic determinants of diaminopimelate and ornithine decarboxylases using alternate substrates

Cited by 13 publications

References 27 publications

Oxygen reactivity with pyridoxal 5′-phosphate enzymes: biochemical implications and functional relevance

Oxygen reactivity with pyridoxal 5′-phosphate enzymes: biochemical implications and functional relevance

Molecular characterization of novel pyridoxal‐5′‐phosphate‐dependent enzymes from the human microbiome

Efficient Production of Enantiopure d-Lysine from l-Lysine by a Two-Enzyme Cascade System

Contact Info

Product

Resources

About