Distribution, industrial applications, and enzymatic synthesis of d-amino acids

2015 ◽  
Vol 99 (8) ◽  
pp. 3341-3349 ◽  
Author(s):  
Xiuzhen Gao ◽  
Qinyuan Ma ◽  
Hailiang Zhu
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis ◽  
Industrial Applications

Enzymatic Synthesis of 15N-L-aspartic Acid Using Recombinant Aspartase from Escherichia Coli K12

2008 ◽  
Vol 59 (11) ◽  
Author(s):  
Iulia Lupan ◽  
Sergiu Chira ◽  
Maria Chiriac ◽  
Nicolae Palibroda ◽  
Octavian Popescu
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Enzymatic Synthesis ◽  
Large Scale ◽  
Recombinant Dna ◽  
Industrial Enzymes ◽  
Recombinant Dna Technology ◽  
Bacterial Fermentation ◽  
Natural Protein ◽  
Novel Method

Amino acids are obtained by bacterial fermentation, extraction from natural protein or enzymatic synthesis from specific substrates. With the introduction of recombinant DNA technology, it has become possible to apply more rational approaches to enzymatic synthesis of amino acids. Aspartase (L-aspartate ammonia-lyase) catalyzes the reversible deamination of L-aspartic acid to yield fumaric acid and ammonia. It is one of the most important industrial enzymes used to produce L-aspartic acid on a large scale. Here we described a novel method for [15N] L-aspartic synthesis from fumarate and ammonia (15NH4Cl) using a recombinant aspartase.

Characterization of an isozyme of S-adenosylmethionine synthetase from rat liver

1984 ◽  
Vol 62 (5) ◽  
pp. 276-279 ◽  
Author(s):  
C. H. Lin ◽  
W. Chung ◽  
K. P. Strickland ◽  
A. J. Hudson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Adenosylmethionine Synthetase ◽  
Cellulose Column

An isozyme of S-adenosylmethionine synthetase has been purified to homogeneity by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and gel filtration on a Sephadex G-200 column. The purified enzyme is very unstable and has a molecular weight of 120 000 consisting of two identical subunits. Amino acid analysis on the purified enzyme showed glycine, glutamate, and aspartate to be the most abundant and the aromatic amino acids to be the least abundant. It possesses tripolyphosphatase activity which can be stimulated five to six times by S-adenosylmethionine (20–40 μM). The findings support the conclusion that an enzyme-bound tripolyphosphate is an obligatory intermediate in the enzymatic synthesis of S-adenosylmethionine from ATP and methionine.

scholarly journals Biosensors for D-Amino Acids: Detection Methods and Applications

2020 ◽  
Vol 21 (13) ◽  
pp. 4574
Author(s):  
Elena Rosini ◽  
Paola D’Antona ◽  
Loredano Pollegioni
Keyword(s):  
Amino Acids ◽  
Industrial Applications ◽  
Detection Methods ◽  
Future Research ◽  
Online Application ◽  
Selective Determination ◽  
Long Time ◽  
Neurological Research ◽  
Review Reports ◽  
Science Investigations

D-enantiomers of amino acids (D-AAs) are only present in low amounts in nature, frequently at trace levels, and for this reason, their biological function was undervalued for a long time. In the past 25 years, the improvements in analytical methods, such as gas chromatography, HPLC, and capillary electrophoresis, allowed to detect D-AAs in foodstuffs and biological samples and to attribute them specific biological functions in mammals. These methods are time-consuming, expensive, and not suitable for online application; however, life science investigations and industrial applications require rapid and selective determination of D-AAs, as only biosensors can offer. In the present review, we provide a status update concerning biosensors for detecting and quantifying D-AAs and their applications for safety and quality of foods, human health, and neurological research. The review reports the main challenges in the field, such as selectivity, in order to distinguish the different D-AAs present in a solution, the simultaneous assay of both L- and D-AAs, the production of implantable devices, and surface-scanning biosensors. These innovative tools will push future research aimed at investigating the neurological role of D-AAs, a vibrant field that is growing at an accelerating pace.

Multi-Enzymatic Synthesis of Optically Pure β-Hydroxy α-Amino Acids

2014 ◽  
Vol 357 (4) ◽  
pp. 767-774 ◽  
Author(s):  
Makoto Hibi ◽  
Takuya Kasahara ◽  
Takashi Kawashima ◽  
Hiroko Yajima ◽  
Shoko Kozono ◽  
...  
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis ◽  
Optically Pure

ChemInform Abstract: Enzymatic Synthesis of Unnatural Amino Acids

ChemInform ◽  
2009 ◽  
Vol 40 (52) ◽  
Author(s):  
Mari Hara Yasuda ◽  
Makoto Ueda ◽  
Kazuya Okano ◽  
Hisaaki Mihara ◽  
Nobuyoshi Esaki
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis ◽  
Unnatural Amino Acids

Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase fromPyrococcussp. ST04

2014 ◽  
Vol 70 (6) ◽  
pp. 1659-1668 ◽  
Author(s):  
Kwang-Hyun Park ◽  
Jong-Hyun Jung ◽  
Sung-Goo Park ◽  
Myeong-Eun Lee ◽  
James F. Holden ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Basis ◽  
Amino Acid Sequence Identity ◽  
Structural Features ◽  
Industrial Applications ◽  
Closed Cavity ◽  
Helical Bundles ◽  
Sequence Identity ◽  
Hydrolysis Of ◽  
Potential Use

A novel maltose-forming α-amylase (PSMA) was recently found in the hyperthermophilic archaeonPyrococcussp. ST04. This enzyme shows <13% amino-acid sequence identity to other known α-amylases and displays a unique enzymatic property in that it hydrolyzes both α-1,4-glucosidic and α-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Here, the crystal structure of PSMA at a resolution of 1.8 Å is reported, showing a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1–341) with a typical GH57 family (β/α)7-barrel fold and a C-domain (amino acids 342–597) composed of α-helical bundles. A small closed cavity observed in proximity to the catalytic residues Glu153 and Asp253 at the domain interface has the appropriate volume and geometry to bind a maltose unit, accounting for the selective exo-type maltose hydrolysis of the enzyme. A narrow gate at the putative subsite +1 formed by residue Phe218 and Phe452 is essential for specific cleavage of glucosidic bonds. The closed cavity at the active site is connected to a short substrate-binding channel that extends to the central hole of the tetramer, exhibiting a geometry that is significantly different from classical maltogenic amylases or β-amylases. The structural features of this novel exo-type maltose-forming α-amylase provide a molecular basis for its unique enzymatic characteristics and for its potential use in industrial applications and protein engineering.

Human acetyl-CoA:glucosamine-6-phosphate N-acetyltransferase 1 has a relaxed donor specificity and transfers acyl groups up to four carbons in length

2016 ◽  
Vol 94 (2) ◽  
pp. 197-204 ◽  
Author(s):  
Inka Brockhausen ◽  
Dileep G. Nair ◽  
Min Chen ◽  
Xiaojing Yang ◽  
John S. Allingham ◽  
...  
Keyword(s):  
Amino Acids ◽  
Articular Cartilage ◽  
Enzymatic Synthesis ◽  
Biomedical Applications ◽  
Binding Pocket ◽  
Wild Type ◽  
Acetyl Coenzyme A ◽  
Site Specific ◽  
Acetyl Group

Glucosamine-6-phosphate N-acetyltransferase1 (GNA1) catalyses the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to glucosamine-6-phosphate (GlcN6P) to form N-acetylglucosamine-6-phosphate (GlcNAc6P), which is an essential intermediate in UDP-GlcNAc biosynthesis. An analog of GlcNAc, N-butyrylglucosamine (GlcNBu) has shown healing properties for bone and articular cartilage in animal models of arthritis. The goal of this work was to examine whether GNA1 has the ability to transfer a butyryl group from butyryl-CoA to GlcN6P to form GlcNBu6P, which can then be converted to GlcNBu. We developed fluorescent and radioactive assays and examined the donor specificity of human GNA1. Acetyl, propionyl, n-butyryl, and isobutyryl groups were all transferred to GlcN6P, but isovaleryl-CoA and decanoyl-CoA did not serve as donor substrates. Site-specific mutants were produced to examine the role of amino acids potentially affecting the size and properties of the AcCoA binding pocket. All of the wild type and mutant enzymes showed activities of both acetyl and butyryl transfer and can therefore be used for the enzymatic synthesis of GlcNBu for biomedical applications.

scholarly journals Cover Picture: Multi-Enzymatic Synthesis of Optically Pure β-Hydroxy α-Amino Acids (Adv. Synth. Catal. 4/2015)

2015 ◽  
Vol 357 (4) ◽  
pp. 605-605
Author(s):  
Makoto Hibi ◽  
Takuya Kasahara ◽  
Takashi Kawashima ◽  
Hiroko Yajima ◽  
Shoko Kozono ◽  
...  
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis ◽  
Optically Pure

scholarly journals The chemo- enzymatic synthesis of labeled l-amino acids and some of their derivatives

2018 ◽  
Vol 317 (2) ◽  
pp. 643-666 ◽  
Author(s):  
Małgorzata Pająk ◽  
Katarzyna Pałka ◽  
Elżbieta Winnicka ◽  
Marianna Kańska
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis

Enzymatic synthesis of α-deuterated amino acids

1996 ◽  
Vol 24 (1) ◽  
pp. 133S-133S ◽  
Author(s):  
John J. Milne ◽  
J. Paul G. Malthouse
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis
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