Identification and analysis of a novel mutation in PEPD gene in two Kashmiri siblings with prolidase enzyme deficiency

Prolidase deficiency (PD) is a rare inborn disorder of collagen metabolism characterized by chronic recurrent cutaneous ulceration. We report a novel 3 bp insertion in the 12th exon of the PEPD gene in two Kashmiri siblings with prolidase deficiency phenotype. This mutation results in addition of an extra alanine residue at the amino-acid position number 304 of prolidase peptide. The structural analysis showed that this Ala insertion is located at the helix (a.a. 300–320), which contains several important hydrogen bonds between residues essential for structural folding for the enzyme activity. In silico analysis suggests that this insertion mutation might distort or bend the helical feature to affect the hydrogen-bond network between residues of neighboring secondary structures and deform the metal-binding geometry of the enzyme. Although approximately 70 PEPD gene mutations and polymorphisms have been reported in various ethnic groups, we however report, for the first time, the identification of insertion mutation in human the PEPD gene.     

Influence of nitrogen source on photochemistry and antenna size of the photosystems in marine green macroalgae,Ulva lactuca

Photosynthesis Research - Ulva lactuca is regarded as a prospective energy crop for biorefinery owing to its affluent biochemical composition and high growth rate. In fast-growing macroalgae,...     

Reduction by a model of NAD(P)H: XXIII. Kinetics for the reduction of 2-acylpyridines

Kinetics for the reduction of 2-acetylpyridine and 2-benzoylpyridine with 1-benzyl-1,4-dihydronicotinamide in acetonitrile has been studied. Isotope effects of the reduction reveal that the transfer of hydrogen nucleus is involved in the rate-determining step. The effect of zinc ion on the reaction rate has been studied quantitatively and the true reacting species have been elucidated.     

Chemical modification of alpha-chymotrypsin for obtaining high transesterification activity in low water organic media

Alpha-chymotrypsin was made more hydrophilic by modifying 11 (out of 16) ε-amino groups with pyromellitic dianhydride. The hydrophilic preparation was precipitated with n-propanol. This preparation gave significantly higher initial rates at the optimum a_w (127.51 nmol mg^?1 min^?1 in n-octane and 21.30 nmol mg^?1 min^?1 in acetonitrile at a_w=0.33) compared with the lyophilized preparation (53.50 nmol mg^?1 min^?1 in n-octane and 0.26 nmol mg^?1 min^?1 in acetonitrile at a_w=0.97). FT-IR showed that the precipitate of modified alpha-chymotrypsin has a higher content of alpha-helices and beta-sheets compared to the lyophilized powder.     

Surface proteome mining for identification of potential vaccine candidates against Campylobacter jejuni: an in silico approach

Functional & Integrative Genomics - Campylobacter jejuni remains a major cause of human gastroenteritis with estimated annual incidence rate of 450 million infections worldwide. C. jejuni is a...