Dataset Information

Lactate racemase proteins MALDI TOF/TOF

ABSTRACT: This project reports the characterization of the lactate racemase system in Lactobacillus plantarum. The lactate racemase (LarA) is a nickel-dependent enzyme. The apo-enzyme (apoLarA) is activated by a single nickel-containing maturation protein (LarE) that requires preactivation by two other accessory proteins (LarC which is a fusion between LarC1 and LarcC2 and LarB). Data submitted here identify the purified forms of Lar proteins.

OTHER RELATED OMICS DATASETS IN: PRJNA186636

INSTRUMENT(S): 4800 Proteomics Analyzer

ORGANISM(S): Lactobacillus Plantarum

SUBMITTER: Pascal Hols

LAB HEAD: MORSOMME Pierre

PROVIDER: PXD000775 | Pride | 2014-04-02

REPOSITORIES: Pride

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Publications

Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system.

Desguin Benoît B Goffin Philippe P Viaene Eric E Kleerebezem Michiel M Martin-Diaconescu Vlad V Maroney Michael J MJ Declercq Jean-Paul JP Soumillion Patrice P Hols Pascal P

Nature communications 20140407

Racemases catalyse the inversion of stereochemistry in biological molecules, giving the organism the ability to use both isomers. Among them, lactate racemase remains unexplored due to its intrinsic instability and lack of molecular characterization. Here we determine the genetic basis of lactate racemization in Lactobacillus plantarum. We show that, unexpectedly, the racemase is a nickel-dependent enzyme with a novel α/β fold. In addition, we decipher the process leading to an active enzyme, wh ...[more]

PMID: 24710389

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Project description:Purpose: Delonix regia or Gulmohor commonly grows here and there in Indian villages as well as it is used for megacity beautification and environmental management due to its evergreen nature and vibrant flower colour. However, an increasing incidence of seasonal pollinosis was observed among the inhabitants living in close vicinity to this tree suggesting a possible link between the airborne pollen load and the concomitant respiratory hazards. This prompted us to investigate the allergens in the pollen of this dominant avenue tree. Methodology: Allergenicity of D. regia pollen grains was first checked by Skin Prick Test (SPT) and further confirmed by in vitro tests, such as, ELISA, Dot Blot and histamine release assay. The total proteome profiling was done by 2D PAGE and it was confronted with the pooled sera of 10 patients. The IgE reactive proteins were identified by MALDI TOF/TOF in Autoflex speed (Bruker,Germany). The raw spectra were searched against NCBInr database using MASCOT search engine. Result: Delonix regia, pollen grains have been found in considerable amount in the air during its flowering season (May to July). Approximately 31% of atopic individuals were found allergic to D. regia, pollen with elevated level of specific IgE and histamine in the serum. Total 8 IgE reactive proteins have been identified by homology driven proteomics. These proteins are ATP synthase beta subunit (spot no 5), Actin (spot no 6), Hypothetical actin like protein (spot no 7), Recombinant S-adenosylmethionine synthase 2 (spot no 9), UDP-arabinopyranose mutase (spot no 13), Luminal-binding 5 (spot no 2), ELF3-like protein (spot no 8) and hypothetical protein OsJ_04810 (spot no 11). Among these eight identified allergenic proteins, five were previously reported as allergen from different sources whereas the rest three have been reported for the first time as novel allergens. Conclusion: Novelty of this study was to identify 8 allergens from D.regia for the first time using immune-biochemical and proteomic techniques. Further studies will open up new avenues in component resolved diagnosis of pollen allergy.

			Action	DRS
	LarA.dat	Other
	LarC.dat	Other
	LarC1.dat	Other
	LarE.dat	Other
	larA.mzXML	Mzxml