Bakeer W

References (2)

Title : Comparative Structural Analysis of Different Mycobacteriophage-Derived Mycolylarabinogalactan Esterases (Lysin B) - Korany_2019_Biomolecules_10_
Author(s) : Korany AH , Abouhmad A , Bakeer W , Essam T , Amin MA , Hatti-Kaul R , Dishisha T
Ref : Biomolecules , 10 : , 2019
Abstract : Mycobacteriophage endolysins have emerged as a potential alternative to the current antimycobacterial agents. This study focuses on mycolylarabinogalactan hydrolase (LysB) enzymes of the alpha/beta-hydrolase family, which disrupt the unique mycolic acid layer of mycobacterium cell wall. Multiple sequence alignment and structural analysis studies showed LysB-D29, the only enzyme with a solved three-dimensional structure, to share several common features with esterases (lacking lid domain) and lipases (acting on long chain lipids). Sequence and structural comparisons of 30 LysB homology models showed great variation in domain organizations and total protein length with major differences in the loop-5 motif harboring the catalytic histidine residue. Docking of different p-nitrophenyl ligands (C4-C18) to LysB-3D models revealed that the differences in length and residues of loop-5 contributed towards wide diversity of active site conformations (long tunnels, deep and superficial funnels, shallow bowls, and a narrow buried cave) resembling that of lipases, cutinases, and esterases. A set of seven LysB enzymes were recombinantly produced; their activity against p-nitrophenyl esters could be related to their active site conformation and acyl binding site. LysB-D29 (long tunnel) showed the highest activity with long chain p-nitrophenyl palmitate followed by LysB-Omega (shallow bowl) and LysB-Saal (deep funnel).
ESTHER : Korany_2019_Biomolecules_10_
PubMedSearch : Korany_2019_Biomolecules_10_
PubMedID: 31892223

Title : Heterologous expression of the avirulence gene ACE1 from the fungal rice pathogen Magnaporthe oryzae - Song_2015_Chem.Sci_6_4837
Author(s) : Song Z , Bakeer W , Marshall JW , Yakasai AA , Khalid RM , Collemare J , Skellam E , Tharreau D , Lebrun MH , Lazarus CM , Bailey AM , Simpson TJ , Cox RJ
Ref : Chem Sci , 6 :4837 , 2015
Abstract : The ACE1 and RAP1 genes from the avirulence signalling gene cluster of the rice blast fungus Magnaporthe oryzae were expressed in Aspergillus oryzae and M. oryzae itself. Expression of ACE1 alone produced a polyenyl pyrone (magnaporthepyrone), which is regioselectively epoxidised and hydrolysed to give different diols, 6 and 7, in the two host organisms. Analysis of the three introns present in ACE1 determined that A. oryzae does not process intron 2 correctly, while M. oryzae processes all introns correctly in both appressoria and mycelia. Co-expression of ACE1 and RAP1 in A. oryzae produced an amide 8 which is similar to the PKS-NRPS derived backbone of the cytochalasans. Biological testing on rice leaves showed that neither the diols 6 and 7, nor amide 8 was responsible for the observed ACE1 mediated avirulence, however, gene cluster analysis suggests that the true avirulence signalling compound may be a tyrosine-derived cytochalasan compound.
ESTHER : Song_2015_Chem.Sci_6_4837
PubMedSearch : Song_2015_Chem.Sci_6_4837
PubMedID: 29142718
Gene_locus related to this paper: phano-phmG , aspcl-CCSE , aspfu-psoB , mago7-ORFZB