![]() Amidase structure
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Common Name | Amidase | ||
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CAS Number | 9012-56-0 | Molecular Weight | N/A | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | N/A | Melting Point | N/A | |
MSDS | USA | Flash Point | N/A |
Escherichia coli glutathionylspermidine synthetase/amidase: phylogeny and effect on regulation of gene expression.
FEMS Microbiol. Lett. 338(2) , 132-40, (2013) Glutathionylspermidine synthetase/amidase (Gss) and the encoding gene (gss) have only been studied in Escherichia coli and several members of the Kinetoplastida phyla. In the present article, we have studied the phylogenetic distribution of Gss and have found... |
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Intermediate accumulation of metabolites results in a bottleneck for mineralisation of the herbicide metabolite 2,6-dichlorobenzamide (BAM) by Aminobacter spp.
Appl. Microbiol. Biotechnol. 94(1) , 237-45, (2012) Degradation and mineralisation of the groundwater contaminant 2,6-dichloro-benzamide (BAM) was investigated in two Aminobacter strains focussing on the induction of BAM degradation and mineralisation and occurrence of intermediate metabolites. The BAM degrada... |
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High-yield continuous production of nicotinic acid via nitrile hydratase-amidase cascade reactions using cascade CSMRs.
Enzyme Microb. Technol. 48(4-5) , 345-50, (2011) High yields of nicotinic acid from 3-cyanopyridine bioconversion were obtained by exploiting the in situ nitrile hydratase-amidase enzymatic cascade system of Microbacterium imperiale CBS 498-74. Experiments were carried out in continuously stirred tank UF-me... |
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Structure-function analysis of Staphylococcus aureus amidase reveals the determinants of peptidoglycan recognition and cleavage.
J. Biol. Chem. 289(16) , 11083-94, (2014) The bifunctional major autolysin AtlA of Staphylococcus aureus cleaves the bacterium's peptidoglycan network (PGN) at two distinct sites during cell division. Deletion of the enzyme results in large cell clusters with disordered division patterns, indicating ... |
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Mycobacteriophage Ms6 LysA: a peptidoglycan amidase and a useful analytical tool.
Appl. Environ. Microbiol. 79(3) , 768-73, (2013) Since the peptidoglycan isolated from Mycobacterium spp. is refractory to commercially available murolytic enzymes, possibly due to the presence of various modifications found on this peptidoglycan, the utility of a mycobacteriophage-derived murolytic enzyme ... |
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Structure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate state.
J. Biol. Chem. 282 , 19598-19605, (2007) Microbial amidases belong to the thiol nitrilases family and have potential biotechnological applications in chemical and pharmaceutical industries as well as in bioremediation. The amidase from Pseudomonas aeruginosa isa6 x 38-kDa enzyme that catalyzes the h... |
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Butyramide-utilizing mutants of Pseudomonas aeruginosa 8602 which produce an amidase with altered substrate specificity.
J. Gen. Microbiol. 57 , 273, (1969)
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Reducing virulence of the human pathogen Burkholderia by altering the substrate specificity of the quorum-quenching acylase PvdQ.
Proc. Natl. Acad. Sci. U. S. A. 111(4) , 1568-73, (2014) The use of enzymes to interfere with quorum sensing represents an attractive strategy to fight bacterial infections. We used PvdQ, an effective quorum-quenching enzyme from Pseudomonas aeruginosa, as a template to generate an acylase able to effectively hydro... |
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Esterases with an introduced amidase-like hydrogen bond in the transition state have increased amidase specificity.
ChemBioChem. 13(5) , 645-8, (2012)
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Transferred interbacterial antagonism genes augment eukaryotic innate immune function.
Nature 518(7537) , 98-101, (2015) Horizontal gene transfer allows organisms to rapidly acquire adaptive traits. Although documented instances of horizontal gene transfer from bacteria to eukaryotes remain rare, bacteria represent a rich source of new functions potentially available for co-opt... |