Results 11 to 20 of about 359 (138)

L-Lysine α-Oxidase: Enzyme with Anticancer Properties

open access: yesPharmaceuticals, 2021
L-lysine α-oxidase (LO), one of L-amino acid oxidases, deaminates L-lysine with the yield of H2O2, ammonia, and α-keto-ε-aminocaproate. Multiple in vitro and in vivo studies have reported cytotoxic, antitumor, antimetastatic, and antitumor activity of LO.
E. V. Lukasheva   +4 more
semanticscholar   +1 more source

Cyclic 68Ga-Labeled Peptides for Specific Detection of Human Angiotensin-Converting Enzyme 2

open access: yesJournal of Nuclear Medicine, 2021
Visual Abstract In this study, we developed angiotensin-converting enzyme 2 (ACE2)–specific, peptide-derived 68Ga-labeled radiotracers, motivated by the hypotheses that ACE2 is an important determinant of severe acute respiratory syndrome coronavirus 2 ...
Matthew F. L. Parker   +5 more
semanticscholar   +1 more source

A High-Efficiency Artificial Synthetic Pathway for 5-Aminovalerate Production From Biobased L-Lysine in Escherichia coli

open access: yesFrontiers in Bioengineering and Biotechnology, 2021
Bioproduction of 5-aminovalerate (5AVA) from renewable feedstock can support a sustainable biorefinery process to produce bioplastics, such as nylon 5 and nylon 56.
Jie Cheng   +6 more
semanticscholar   +1 more source

Structural basis of strict substrate recognition of l‐lysine α‐oxidase from Trichoderma viride

open access: yesProtein Science, 2020
l‐Lysine oxidase (LysOX) is a FAD‐dependent homodimeric enzyme that catalyzes the oxidative deamination of l‐lysine to produce α‐keto‐ε‐aminocaproate with ammonia and hydrogen peroxide.
H. Kondo   +9 more
semanticscholar   +1 more source

Cyclic gallium-68 labeled peptides for specific detection of human angiotensin-converting enzyme 2

open access: yesbioRxiv, 2020
In this study, we developed ACE2-specific, peptide-derived 68Ga-labeled radiotracers, motivated by the hypotheses that (1) ACE2 is an important determinant of SARS-CoV-2 susceptibility, and (2) that modulation of ACE2 in COVID-19 drives severe organ ...
Matthew F. L. Parker   +5 more
semanticscholar   +1 more source

Production of nonnatural straight-chain amino acid 6-aminocaproate via an artificial iterative carbon-chain-extension cycle

open access: yesbioRxiv, 2019
Bioplastics produced from microbial source are promising green alternatives to traditional petrochemical-derived plastics. Nonnatural straight-chain amino acids, especially 5-aminovalerate, 6-aminocaproate and 7-aminoheptanoate are potential monomers for
Jie Cheng   +7 more
semanticscholar   +1 more source

Characterization of a neutral protease from lysosomes of rabbit polymorphonuclear leucocytes.

open access: yesBiochemical Journal, 1971
1. The subcellular distribution has been investigated of a protease from rabbit polymorphonuclear leucocytes, obtained from peritoneal exudates. The enzyme, optimally active between pH7.0 and 7.5, hydrolyses histone but not haemoglobin, sediments almost ...
Philip Davies   +3 more
semanticscholar   +1 more source

Novel Degradation Pathway of Glycated Amino Acids into Free Fructosamine by a Pseudomonas sp. Soil Strain Extract (*)

open access: yesJournal of Biological Chemistry, 1995
A Pseudomonas sp. soil strain, selected for its ability to grow on -(1-deoxyfructosyl) aminocaproic acid, was induced to express a membrane-bound enzymatic activity which oxidatively degrades Amadori products into free fructosamine. Apparent K values for
C. Gerhardinger   +4 more
semanticscholar   +1 more source

Purification and Characterization of a Membrane-bound Deglycating Enzyme (1-Deoxyfructosyl Alkyl Amino Acid Oxidase, EC 1.5.3) from a Pseudomonas sp. Soil Strain*

open access: yesJournal of Biological Chemistry, 1996
Searching for novel approaches for uncoupling glycation from hyperglycemia as a cause of diabetic complications, a Pseudomonas sp. soil strain containing a membrane-bound enzyme that deglycates amino acids under release of free fructosamine was isolated (
A. K. Saxena, P. Saxena, V. Monnier
semanticscholar   +1 more source

Diversity at the variable-joining region boundary of lambda light chains has a pronounced effect on immunoglobulin ligand-binding activity.

open access: yesProceedings of the National Academy of Sciences of the United States of America, 1984
By recombining lambda light (L) chains having known variable (V) region amino acid or nucleotide sequences with a heavy (H) chain from a myeloma protein or a monoclonal antibody, we obtained reconstituted Igs that differed from each other in sequence by ...
T. Azuma, V. Igras, E. Reilly, H. Eisen
semanticscholar   +1 more source

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