(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Bacillales: NE > Bacillaceae: NE > Bacillus: NE > Bacillus megaterium: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Priestia megaterium: N, E.
Bacillus megaterium WSH-002: N, E.
Bacillus megaterium NBRC 15308 = ATCC 14581: N, E.
Bacillus megaterium Q3: N, E.
Bacillus megaterium DSM 319: N, E.
Bacillus megaterium QM B1551: N, E.
Molecular evidence
Database
No mutation 4 structures(e.g. : 4INZ, 4IO0, 4NZZ... more)(less) 4INZ: The crystal structure of M145A mutant of an epoxide hydrolase from Bacillus megaterium, 4IO0: Crystal structure of F128A mutant of an epoxide hydrolase from Bacillus megaterium complexed with its product (R)-3-[1]naphthyloxy-propane-1,2-diol, 4NZZ: Crystal structure of bacillus megaterium epoxide hydrolase, 4O08: Crystal structure of bacillus megaterium epoxide hydrolase in complex with 2-Phenoxyacetamide No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA GSHMASMTGGQQMGRGSMSKQYINVNGVNLHYISKGQGELMLFLHGFPDF SHIWRHQIDEFSNDFHTVALDLRGYNLSEKPSGLESYEIDVLVEDIRQVI EGLGYSSCTLVVHDWGAGIGWTFAYRYPEYVQKLIAFNGPHPYTFMRELR TNKNQQKASEYAKWFQKQEVQDYMERDNFSGLRKLVIDPGVKKGYLTADD VQAYMNSWENGSVLSMLSYYRNLKIFTEEDLRRKSLFPLEEEVLNIPVQI IWGNQDPTFMPENLDGIEEYVPNISVHRLAEASHAPQHEKPQEVNNVMWN FLNK
References
Title: Engineering of an epoxide hydrolase for efficient bioresolution of bulky pharmaco substrates Kong XD, Yuan S, Li L, Chen S, Xu JH, Zhou J Ref: Proc Natl Acad Sci U S A, 111:15717, 2014 : PubMed
Optically pure epoxides are essential chiral precursors for the production of (S)-propranolol, (S)-alprenolol, and other beta-adrenergic receptor blocking drugs. Although the enzymatic production of these bulky epoxides has proven difficult, here we report a method to effectively improve the activity of BmEH, an epoxide hydrolase from Bacillus megaterium ECU1001 toward alpha-naphthyl glycidyl ether, the precursor of (S)-propranolol, by eliminating the steric hindrance near the potential product-release site. Using X-ray crystallography, mass spectrum, and molecular dynamics calculations, we have identified an active tunnel for substrate access and product release of this enzyme. The crystal structures revealed that there is an independent product-release site in BmEH that was not included in other reported epoxide hydrolase structures. By alanine scanning, two mutants, F128A and M145A, targeted to expand the potential product-release site displayed 42 and 25 times higher activities toward alpha-naphthyl glycidyl ether than the wild-type enzyme, respectively. These results show great promise for structure-based rational design in improving the catalytic efficiency of industrial enzymes for bulky substrates.
Bacillus megaterium, an industrial strain, has been widely used in protein production and the vitamin C industry. Here we reported a finished, annotated, and compared 4.14-Mbp high-quality genome sequence of B. megaterium WSH-002, which is the companion strain for Ketogulonicigenium vulgare in the vitamin C industry and is stocked in our laboratory.
Title: Improved catalytic performance of Bacillus megaterium epoxide hydrolase in a medium containing Tween-80 Gong PF, Xu JH, Tang YF, Wu HY Ref: Biotechnol Prog, 19:652, 2003 : PubMed
A new epoxide hydrolase with high enantioselectivity toward (R)-glycidyl phenyl ether (R-GPE) was partially purified from Bacillus megaterium strain ECU1001. The maximum activity of the isolated enzyme was observed at 30 degrees C and pH 6.5 in a buffer system with 5% (v/v) of DMSO as a cosolvent. The enzyme was quite stable at pH 7.5 and retained full activity after incubation at 40 degrees C for 6 h. Interestingly, when the cosolvent DMSO was replaced by an emulsifier (Tween-80, 0.5% w/v) as an alternative additive to help disperse the water-insoluble substrate, the apparent activity of the epoxide hydrolase significantly increased by about 1.8-fold, while the temperature optimum shifted from 30 to 40 degrees C and the half-life of the enzyme at 50 degrees C increased by 2.5 times. The enzymatic hydrolysis of rac-GPE was highly enantioselective, with an E-value (enantiomeric ratio) of 69.3 in the Tween-80 emulsion system, which is obviously higher than that (41.2) observed in the DMSO-containing system.
Bacillus megaterium Soluble epoxide hydrolase
