Chirality-specific hydrolysis of amino acid substrates by cellulose nanofibers

A new series of amino acid derivatives of quinolines was synthesized through the hydrolysis of amino acid methyl esters of quinoline carboxamides with alkali hydroxide. The compounds were purified on silica gel by column chromatography and further characterized by TLC, NMR and ESI-TOF mass spectrometry. All compounds were screened for in vitro antimicrobial activity against different bacterial strains using the microdilution method. Most of the synthesized amino acid-quinolines show more potent or equipotent inhibitory action against the tested bacteria than their correspond esters. In addition, many of them exhibit fluorescent properties and could possibly be utilized as fluorophores. Molecular docking and simulation studies of the compounds at putative bacterial target enzymes suggest that the antimicrobial potency of these synthesized analogues could be due to enzyme inhibition via their favorable binding at the fluoroquinolone binding site at the GyrA subunit of DNA gyrase and/or the ParC subunit of topoisomerase-IV.

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ChemInform Abstract: Perfect Enantioselective Hydrolysis of Amino Acid Esters by Modified . alpha.-Chymotrypsin.

ChemInform ◽

10.1002/chin.199521237 ◽

2010 ◽

Vol 26 (21) ◽

pp. no-no

Author(s):

R. UEOKA ◽

J. OKAI ◽

K. SHIMADA ◽

D. SEGAWA ◽

T. NAKATA ◽

...

Keyword(s):

Amino Acid ◽

Enantioselective Hydrolysis ◽

Amino Acid Esters ◽

Hydrolysis Of ◽

Acid Esters

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GES-2, a Class A β-Lactamase fromPseudomonas aeruginosa with Increased Hydrolysis of Imipenem

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.45.9.2598-2603.2001 ◽

2001 ◽

Vol 45 (9) ◽

pp. 2598-2603 ◽

Cited By ~ 139

Author(s):

Laurent Poirel ◽

Gerhard F. Weldhagen ◽

Thierry Naas ◽

Christophe De Champs ◽

Michael G. Dove ◽

...

Keyword(s):

Escherichia Coli ◽

Pseudomonas Aeruginosa ◽

Amino Acid ◽

Amino Acid Change ◽

Blood Cultures ◽

Class A ◽

Omega Loop ◽

Cephalosporin Resistance ◽

Lactamase Gene ◽

Hydrolysis Of

ABSTRACT Pseudomonas aeruginosa GW-1 was isolated in 2000 in South Africa from blood cultures of a 38-year-old female who developed nosocomial pneumonia. This isolate harbored a self-transferable ca. 100-kb plasmid that conferred an expanded-spectrum cephalosporin resistance profile associated with an intermediate susceptibility to imipenem. A β-lactamase gene, bla GES-2, was cloned from whole-cell DNA of P. aeruginosa GW-1 and expressed in Escherichia coli. GES-2, with a pI value of 5.8, hydrolyzed expanded-spectrum cephalosporins, and its substrate profile was extended to include imipenem compared to that of GES-1, identified previously in Klebsiella pneumoniae. GES-2 activity was less inhibited by clavulanic acid, tazobactam and imipenem than GES-1. The GES-2 amino acid sequence differs from that of GES-1 by a glycine-to-asparagine substitution in position 170 located in the omega loop of Ambler class A enzymes. This amino acid change may explain the extension of the substrate profile of the plasmid-encoded β-lactamase GES-2.

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A kinetic study of the acid autoxidation of tryptophan

Australian Journal of Chemistry ◽

10.1071/ch9722139 ◽

1972 ◽

Vol 25 (10) ◽

pp. 2139 ◽

Cited By ~ 8

Author(s):

M Stewart ◽

CH Nicholls

Keyword(s):

Free Radical ◽

Amino Acid ◽

Kinetic Study ◽

Acid Hydrolysis ◽

Soda Glass ◽

Glass Containers ◽

Hydrolysis Of

The decomposition of tryptophan in aqueous HC1 at 100�C has been shown to proceed by a free-radical autoxidation mechanism. The acid functions by protonating the amino acid at either the 1- or 3-positions prior to autoxidation and so 1-methyltryptophan is also decomposed under these conditions. Impurities present in the soda glass containers used are shown to be responsible for the initiation of the reaction. The decomposition of tryptophan during the acid hydrolysis of proteins is considered in the light of these results.

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Sub-critical water hydrolysis of hog hair for amino acid production

Bioresource Technology ◽

10.1016/j.biortech.2009.11.054 ◽

2010 ◽

Vol 101 (7) ◽

pp. 2472-2476 ◽

Cited By ~ 32

Author(s):

M.B. Esteban ◽

A.J. García ◽

P. Ramos ◽

M.C. Márquez

Keyword(s):

Amino Acid ◽

Acid Production ◽

Amino Acid Production ◽

Water Hydrolysis ◽

Hydrolysis Of

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Molecular Cloning and Characterization of Bifidobacterium bifidum 1,2-α-l-Fucosidase (AfcA), a Novel Inverting Glycosidase (Glycoside Hydrolase Family 95)

Journal of Bacteriology ◽

10.1128/jb.186.15.4885-4893.2004 ◽

2004 ◽

Vol 186 (15) ◽

pp. 4885-4893 ◽

Cited By ~ 154

Author(s):

Takane Katayama ◽

Akiko Sakuma ◽

Takatoshi Kimura ◽

Yutaka Makimura ◽

Jun Hiratake ◽

...

Keyword(s):

Amino Acid ◽

Genomic Library ◽

Bifidobacterium Bifidum ◽

Glycoside Hydrolases ◽

Glycoside Hydrolase Family ◽

Amino Acid Residues ◽

Gene Encoding ◽

Sugar Chain ◽

Hydrolysis Of

ABSTRACT A genomic library of Bifidobacterium bifidum constructed in Escherichia coli was screened for the ability to hydrolyze the α-(1→2) linkage of 2′-fucosyllactose, and a gene encoding 1,2-α-l-fucosidase (AfcA) was isolated. The afcA gene was found to comprise 1,959 amino acid residues with a predicted molecular mass of 205 kDa and containing a signal peptide and a membrane anchor at the N and C termini, respectively. A domain responsible for fucosidase activity (the Fuc domain; amino acid residues 577 to 1474) was localized by deletion analysis and then purified as a hexahistidine-tagged protein. The recombinant Fuc domain specifically hydrolyzed the terminal α-(1→2)-fucosidic linkages of various oligosaccharides and a sugar chain of a glycoprotein. The stereochemical course of the hydrolysis of 2′-fucosyllactose was determined to be inversion by using 1H nuclear magnetic resonance. The primary structure of the Fuc domain exhibited no similarity to those of any glycoside hydrolases (GHs) but showed high similarity to those of several hypothetical proteins in a database. Thus, it was revealed that the AfcA protein constitutes a novel inverting GH family (GH family 95).

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