scholarly journals Biochemical characterization of the water-soluble squalene synthase fromMethylococcus capsulatusand the functional analyses of its two DXXD(E)D motifs and the highly conserved aromatic amino acid residues

FEBS Journal ◽  
2014 ◽  
Vol 281 (24) ◽  
pp. 5479-5497 ◽  
Author(s):  
Kana Ohtake ◽  
Naoki Saito ◽  
Satoshi Shibuya ◽  
Wakako Kobayashi ◽  
Ryosuke Amano ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Biochemical Characterization ◽  
Squalene Synthase ◽  
Water Soluble ◽  
Amino Acid Residues ◽  
Functional Analyses

scholarly journals Biochemical Characterization of Aspergillus fumigatus AroH, a Putative Aromatic Amino Acid Aminotransferase

2018 ◽  
Vol 5 ◽  
Author(s):  
Mirco Dindo ◽  
Egidia Costanzi ◽  
Marco Pieroni ◽  
Claudio Costantini ◽  
Giannamaria Annunziato ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aspergillus Fumigatus ◽  
Aromatic Amino Acid ◽  
Biochemical Characterization ◽  
Aromatic Amino Acid Aminotransferase

Biochemical studies on pili isolated from Pseudomonas aeruginosa strain PAO

1979 ◽  
Vol 25 (10) ◽  
pp. 1175-1181 ◽  
Author(s):  
W. Paranchych ◽  
P. A. Sastry ◽  
L. S. Frost ◽  
M. Carpenter ◽  
G. D. Armstrong ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Biochemical Characterization ◽  
Average Length ◽  
Amino Terminus ◽  
Amino Acid Residues ◽  
Present Communication ◽  
Amino Terminal ◽  
Single Polypeptide

Pseudomonas aeruginosa strains PAO and PAK bear polar pili which are flexible filaments having a diameter of 6 nm and an average length of 2500 nm. Both types of pili are retractile and promote infection by a number of bacteriophages. The present communication describes the partial biochemical characterization of PAO pili isolated from a multipiliated nonretractile mutant of PAO. The observed properties are compared to those of PAK pili which were characterized previously. PAO pili were found to contain a single polypeptide subunit of 18 700 daltons. This is similar to PAK pili which contain a single polypeptide of 18 100 daltons. The amino acid composition of PAO pilin was also similar to that of PAK pilin. Neither protein contained phosphate or carbohydrate residues and both were found to contain N-methylphenylalanine at the amino terminus. Sequencing of 20 amino acid residues at the amino terminal end of PAO pilin revealed the sequence to be identical with that of PAK pilin, while tryptic peptide analyses of PAO and PAK pilin indicated that the two proteins probably contain a number of homologous regions within the polypeptide. It was concluded that PAO and PAK pili are closely related structures.

scholarly journals Biochemical Characterization of a Prokaryotic Phenylalanine Ammonia Lyase

2005 ◽  
Vol 187 (12) ◽  
pp. 4286-4289 ◽  
Author(s):  
Longkuan Xiang ◽  
Bradley S. Moore
Keyword(s):  
Amino Acid ◽  
Cinnamic Acid ◽  
Marine Bacterium ◽  
Phenylalanine Ammonia Lyase ◽  
Biochemical Characterization ◽  
The Novel ◽  
Amino Acid Residues ◽  
Primary Amino ◽  
Biochemical Features

ABSTRACT The committed biosynthetic reaction to benzoyl-coenzyme A in the marine bacterium “Streptomyces maritimus” is carried out by the novel prokaryotic phenylalanine ammonia lyase (PAL) EncP, which converts the primary amino acid l-phenylalanine to trans-cinnamic acid. Recombinant EncP is specific for l-phenylalanine and shares many biochemical features with eukaryotic PALs, which are substantially larger proteins by ∼200 amino acid residues.

Biochemical characterization of HIV-1 reverse transcriptases encoding mutations at amino acid residues 161 and 208 involved in resistance to phosphonoformate

1998 ◽  
Vol 56 (12) ◽  
pp. 1583-1589 ◽  
Author(s):  
Enzo Tramontano ◽  
Giovanna Piras ◽  
John W Mellors ◽  
Monica Putzolu ◽  
Hengameh Z Bazmi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biochemical Characterization ◽  
Amino Acid Residues ◽  
Reverse Transcriptases ◽  
Hiv 1

Properties of a non collagen-degradingBacillus subtiliskeratinase

2008 ◽  
Vol 54 (3) ◽  
pp. 180-188 ◽  
Author(s):  
Alexandre José Macedo ◽  
Walter Orlando Beys da Silva ◽  
Carlos Termignoni
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Molecular Mass ◽  
Biochemical Characterization ◽  
Detectable Effect ◽  
Amino Acid Residues ◽  
Keratinolytic Activity ◽  
Biotechnological Potential ◽  
Optimum Ph

Bacillus subtilis S14 produces a keratinase (KerS14) with non collagen-degrading activity. Indeed, this is the first keratinase described so far that does not have any detectable effect on collagen, which is a crucial property for an enzyme intended to be used in skin dehairing. Because of its importance as an industrial tanning enzyme, we report the biochemical characterization of KerS14. This protein exhibited an apparent molecular mass of 27 kDa, a pI of 6.5, and an optimum pH in the range of 8.0–9.0. The enzyme’s activity was stimulated by Mn2+(7.7-fold), Ca2+(6.1-fold), Mg2+(4.9-fold), and Co2+(4.0-fold) but was inhibited by Cu2+and Zn2+. Using p-nitroanilide and methylcoumarine derivatized peptides, we observed that KerS14 prefered Arg at subsite P1, small amino acid residues at subsite P2, and Gln or Glu at subsite P3. KerS14 presented higher keratin degradation specificity than other commercial proteases. Its high keratinolytic activity and the absence of virtually any activity against collagen remark the biotechnological potential of this enzyme to be used at larger scales in tannery dehairing processes.

scholarly journals Identification and characterization of amphibian SLC26A5 using RNA-Seq

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Zhongying Wang ◽  
Qixuan Wang ◽  
Hao Wu ◽  
Zhiwu Huang
Keyword(s):  
Amino Acid ◽  
Inner Ear ◽  
Hair Cells ◽  
Rana Catesbeiana ◽  
Site Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Rna Seq ◽  
American Bullfrog ◽  
Frog Species

Abstract Background Prestin (SLC26A5) is responsible for acute sensitivity and frequency selectivity in the vertebrate auditory system. Limited knowledge of prestin is from experiments using site-directed mutagenesis or domain-swapping techniques after the amino acid residues were identified by comparing the sequence of prestin to those of its paralogs and orthologs. Frog prestin is the only representative in amphibian lineage and the studies of it were quite rare with only one species identified. Results Here we report a new coding sequence of SLC26A5 for a frog species, Rana catesbeiana (the American bullfrog). In our study, the SLC26A5 gene of Rana has been mapped, sequenced and cloned successively using RNA-Seq. We measured the nonlinear capacitance (NLC) of prestin both in the hair cells of Rana’s inner ear and HEK293T cells transfected with this new coding gene. HEK293T cells expressing Rana prestin showed electrophysiological features similar to that of hair cells from its inner ear. Comparative studies of zebrafish, chick, Rana and an ancient frog species showed that chick and zebrafish prestin lacked NLC. Ancient frog’s prestin was functionally different from Rana. Conclusions We mapped and sequenced the SLC26A5 of the Rana catesbeiana from its inner ear cDNA using RNA-Seq. The Rana SLC26A5 cDNA was 2292 bp long, encoding a polypeptide of 763 amino acid residues, with 40% identity to mammals. This new coding gene could encode a functionally active protein conferring NLC to both frog HCs and the mammalian cell line. While comparing to its orthologs, the amphibian prestin has been evolutionarily changing its function and becomes more advanced than avian and teleost prestin.

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