Amino Acids from Mushrooms

Hatanaka, Shin–ichi

doi:10.1007/978-3-7091-9150-7_1

Cited by 9 publications

(5 citation statements)

References 364 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several chlorinated amino acids are present in fungi [ 87 ]. For example, Amanita solitaria , which has a high chloride concentration, contains 2-amino-5-chloro-hex-4Z-enoic acid ( 23 ), and the antibacterial amino acid (( S )-2-amino-4-chloropent-4-enoic acid, 24 ) was isolated from Amanita pseudoporphyria [ 88 ].…”

Section: Halo-amino Acids and Halogenated Non-ribosomal Peptidesmentioning

confidence: 99%

Natural and Synthetic Halogenated Amino Acids—Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics

Mardirossian

Rubini

Adamo³

et al. 2021

Molecules

View full text Add to dashboard Cite

The 3D structure and surface characteristics of proteins and peptides are crucial for interactions with receptors or ligands and can be modified to some extent to modulate their biological roles and pharmacological activities. The introduction of halogen atoms on the side-chains of amino acids is a powerful tool for effecting this type of tuning, influencing both the physico-chemical and structural properties of the modified polypeptides, helping to first dissect and then rationally modify features that affect their mode of action. This review provides examples of the influence of different types of halogenation in amino acids that replace native residues in proteins and peptides. Examples of synthetic strategies for obtaining halogenated amino acids are also provided, focusing on some representative compounds and their biological effects. The role of halogenation in native and designed antimicrobial peptides (AMPs) and their mimetics is then discussed. These are in the spotlight for the development of new antimicrobial drugs to counter the rise of antibiotic-resistant pathogens. AMPs represent an interesting model to study the role that natural halogenation has on their mode of action and also to understand how artificially halogenated residues can be used to rationally modify and optimize AMPs for pharmaceutical purposes.

show abstract

Section: Halo-amino Acids and Halogenated Non-ribosomal Peptidesmentioning

confidence: 99%

Natural and Synthetic Halogenated Amino Acids—Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics

Mardirossian

Rubini

Adamo³

et al. 2021

Molecules

View full text Add to dashboard Cite

show abstract

“…S1). Its enzymatic activity, expressed as lmoles of p-nitroaniline liberated through the transpeptidation reaction with GPNA as the donor and glycylglycine as the acceptor at pH 8.5 and 22°C [32][33][34][35][36][37][38][39][40][41] pH-activity profile pH-rate profiles for the hydrolase and the transpeptidase activities were determined with the standard method, with GPNA as the donor and glycylglycine as the acceptor [13,32,41]. We found that the hydrolase activity reached a maximum at a pH of~9, and then decreased, giving a bell-shaped curve.…”

Section: Resultsmentioning

confidence: 99%

“…S1). Its enzymatic activity, expressed as lmoles of p-nitroaniline liberated through the transpeptidation reaction with GPNA as the donor and glycylglycine as the acceptor at pH 8.5 and 22°C [32][33][34][35][36][37][38][39][40][41], was calculated to be 18.33 UÁmL À1 enzyme solution. The protein content, measured with the method of Bradford [42], was found to be 34.4 mgÁmL À1 .…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

pH‐Dependent hydrolase, glutaminase, transpeptidase and autotranspeptidase activities of Bacillus subtilis γ‐glutamyltransferase

et al. 2013

View full text Add to dashboard Cite

c-Glutamyltransferases (c-GTs) are heterodimeric enzymes that catalyze the transfer of a c-glutamyl group from a donor species to an acceptor molecule in a transpeptidation reaction through the formation of an intermediate c-glutamyl enzyme. In our search for a c-GT from a generally recognized as safe microorganism suitable for the production of c-glutamyl derivatives with flavor-enhancing properties intended for human use, we cloned and overexpressed the c-GT from Bacillus subtilis. In this study, we report the behavior of B. subtilis c-GT in reactions involving glutamine as the donor compound and various acceptor amino acids. The common thread emerging from our results is a strong dependence of the hydrolase, transpeptidase and autotranspeptidase activities of B. subtilis c-GT on pH, also in relation to the pK a of the acceptor amino acids. Glutamine, commonly referred to as a poor acceptor molecule, undergoes rapid autotranspeptidation at elevated pH, affording oligomeric species, in which up to four c-glutamyl moieties are linked to a single glutamine. Moreover, we found that D-glutamine is also recognized both as a donor and as an acceptor substrate. Our results prove that the B. subtilis c-GT-catalyzed transpeptidation reaction is feasible, and the observed activities of c-GT from B. subtilis could be interpreted in relation to the known ability of the enzyme to process the polymeric material c-polyglutamic acid.

show abstract

“…They also are structural analogs of the synthetic energetic materials nitroguanidine and dinitrourea. Agaricus subrutilescens also produces two other nitramines, L-4-nitramino-2-aminobutanoic acid and the ␥-glutamyl peptide of NEDA (6,9), but little is known about their biological activities. Synthetic cyclic nitramines such as hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX), octahydro-1,3,5,7-tetranitro-1,3,5,7-tetrazocine (HMX), and 2,4,6,8,10,12-hexanitro-2, 4,6,8,10, are explosives used by the military in high-yield munitions.…”

Section: N -Nitroglycine ([Nng] Nitraminoacetic Acid) Is a Nitramine mentioning

confidence: 99%

Iron-Dependent Enzyme Catalyzes the Initial Step in Biodegradation of N -Nitroglycine by Variovorax sp. Strain JS1663

Mahan

Zheng

Fida

et al. 2017

Appl Environ Microbiol

View full text Add to dashboard Cite

Nitramines are key constituents of most of the explosives currently in use and consequently contaminate soil and groundwater at many military facilities around the world. Toxicity from nitramine contamination poses a health risk to plants and animals. Thus, understanding how nitramines are biodegraded is critical to environmental remediation. The biodegradation of synthetic nitramine compounds such as hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) has been studied for decades, but little is known about the catabolism of naturally produced nitramine compounds. In this study, we report the isolation of a soil bacterium, Variovorax sp. strain JS1663, that degrades N-nitroglycine (NNG), a naturally produced nitramine, and the key enzyme involved in its catabolism. Variovorax sp. JS1663 is a Gram-negative, non-sporeforming motile bacterium isolated from activated sludge based on its ability to use NNG as a sole growth substrate under aerobic conditions. A single gene (nnlA) encodes an iron-dependent enzyme that releases nitrite from NNG through a proposed ␤-elimination reaction. Bioinformatics analysis of the amino acid sequence of NNG lyase identified a PAS (Per-Arnt-Sim) domain. PAS domains can be associated with heme cofactors and function as signal sensors in signaling proteins. This is the first instance of a PAS domain present in a denitration enzyme. The NNG biodegradation pathway should provide the basis for the identification of other enzymes that cleave the NON bond and facilitate the development of enzymes to cleave similar bonds in RDX, nitroguanidine, and other nitramine explosives. IMPORTANCEThe production of antibiotics and other allelopathic chemicals is a major aspect of chemical ecology. The biodegradation of such chemicals can play an important ecological role in mitigating or eliminating the effects of such compounds. N-Nitroglycine (NNG) is produced by the Gram-positive filamentous soil bacterium Streptomyces noursei. This study reports the isolation of a Gram-negative soil bacterium, Variovorax sp. strain JS1663, that is able to use NNG as a sole growth substrate. The proposed degradation pathway occurs via a ␤-elimination reaction that releases nitrite from NNG. The novel NNG lyase requires iron(II) for activity. The identification of a novel enzyme and catabolic pathway provides evidence of a substantial and underappreciated flux of the antibiotic in natural ecosystems. Understanding the NNG biodegradation pathway will help identify other enzymes that cleave the NON bond and facilitate the development of enzymes to cleave similar bonds in synthetic nitramine explosives.

show abstract

Amino Acids from Mushrooms

Cited by 9 publications

References 364 publications

Natural and Synthetic Halogenated Amino Acids—Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics

Natural and Synthetic Halogenated Amino Acids—Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics

pH‐Dependent hydrolase, glutaminase, transpeptidase and autotranspeptidase activities of Bacillus subtilis γ‐glutamyltransferase

Iron-Dependent Enzyme Catalyzes the Initial Step in Biodegradation of N -Nitroglycine by Variovorax sp. Strain JS1663

Contact Info

Product

Resources

About