scholarly journals RETRACTION: Immunohistochemical and Functional Characterization of Peptide, Organic Cation, Neutral and Basic Amino Acid, and Monocarboxylate Drug Transporters in Human Ocular Tissues

2012 ◽  
Vol 41 (2) ◽  
pp. 466-474 ◽  
Author(s):  
Rajendra S. Kadam ◽  
Sunil K. Vooturi ◽  
Uday B. Kompella
Keyword(s):  
Amino Acid ◽  
Organic Cation ◽  
Drug Transporters ◽  
Functional Characterization ◽  
Basic Amino Acid ◽  
Ocular Tissues

scholarly journals Identification of a novel subfamily of bacterial AAT-fold basic amino acid decarboxylases and functional characterization of its first representative:Pseudomonas aeruginosaLdcA

2018 ◽  
Author(s):  
Diego Carriel-Lopez ◽  
Pierre Simon Garcia ◽  
Florence Castelli ◽  
Patricia Lamourette ◽  
François Fenaille ◽  
...  
Keyword(s):  
Amino Acid ◽  
Functional Characterization ◽  
Acid Stress ◽  
Basic Amino Acid ◽  
Multidrug Resistant ◽  
Human Pathogen ◽  
Short Forms ◽  
Charged Macromolecules ◽  
Functionally Diverse

SummaryPolyamines are small amino-acid derived polycations capable of binding negatively charged macromolecules. Bacterial polyamines are structurally and functionally diverse, and are mainly produced biosynthetically by PLP-dependent amino acid decarboxylases referred to as LAOdcs (Lysine-Arginine-Ornithine decarboxylases). In a phylogenetically limited group of bacteria, LAOdcs are also induced in response to acid stress. Here, we performed an exhaustive phylogenetic analysis of the AAT-fold LAOdcs which showcased the ancestral nature of their short forms inCyanobacteriaandFirmicutes,and emergence of distinct subfamilies of long LAOdcs inProteobacteria.We identified a novel subfamily of lysine decarboxylases, LdcA, ancestral inBetaproteobacteriaandPseudomortadaceae {Gammaproteobacteria).We analyzed the expression of LdcA fromPseudomonas aeruginosa,and uncovered its role, intimately linked to cadaverine production, in promoting growth and reducing persistence of this multidrug resistant human pathogen during carbenicillin treatment. Finally, we documented a certain redundancy in the function of the three main polyamines - cadaverine, putrescine and spermidine - inP. aeruginosaby demonstrating the link between their intracellular level, as well as the capacity of putrescine and spermidine to complement the growth phenotype of theIdcAmutant.

scholarly journals Regiodivergent Biocatalytic Hydroxylation of L-Glutamine Facilitated by Characterization of Non-Heme Dioxygenases from Non-Ribosomal Peptide Biosyntheses

2021 ◽  
Author(s):  
Hans Renata ◽  
Emily Shimizu ◽  
Christian Zwick
Keyword(s):  
Amino Acid ◽  
Building Block ◽  
Solid Phase ◽  
Functional Characterization ◽  
Free Standing ◽  
Substrate Specificities ◽  
Total Turnover

We report the functional characterization of two iron- and a-ketoglutarate-dependent dioxygenases that are capable of hydroxylating free-standing glutamine at its C3 and C4 position respectively. In particular, the C4 hydroxylase, Q4Ox, catalyzes the reaction with approximately 4,300 total turnover numbers, facilitating synthesis of a solid-phase compatible building block and stereochemical elucidation at the C4 position of the hydroxylated product. This work will enable the development of novel synthetic strategies to prepare useful glutamine derivatives and stimulate further discoveries of new amino acid hydroxylases with distinct substrate specificities.<br>

scholarly journals Regiodivergent Biocatalytic Hydroxylation of L-Glutamine Facilitated by Characterization of Non-Heme Dioxygenases from Non-Ribosomal Peptide Biosyntheses

2021 ◽  
Author(s):  
Hans Renata ◽  
Emily Shimizu ◽  
Christian Zwick
Keyword(s):  
Amino Acid ◽  
Building Block ◽  
Solid Phase ◽  
Functional Characterization ◽  
Free Standing ◽  
Substrate Specificities ◽  
Total Turnover

We report the functional characterization of two iron- and a-ketoglutarate-dependent dioxygenases that are capable of hydroxylating free-standing glutamine at its C3 and C4 position respectively. In particular, the C4 hydroxylase, Q4Ox, catalyzes the reaction with approximately 4,300 total turnover numbers, facilitating synthesis of a solid-phase compatible building block and stereochemical elucidation at the C4 position of the hydroxylated product. This work will enable the development of novel synthetic strategies to prepare useful glutamine derivatives and stimulate further discoveries of new amino acid hydroxylases with distinct substrate specificities.<br>

scholarly journals Characterization of the rat neutral and basic amino acid transporter utilizing anti-peptide antibodies.

1993 ◽  
Vol 90 (9) ◽  
pp. 4022-4026 ◽  
Author(s):  
R. Mosckovitz ◽  
N. Yan ◽  
E. Heimer ◽  
A. Felix ◽  
S. S. Tate ◽  
...  
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Amino Acid Transporter ◽  
Acid Transporter ◽  
Peptide Antibodies
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