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Related Concept Videos

Amino acids03:42

Amino acids

72.9K
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...
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Structure of Amines01:19

Structure of Amines

2.5K
The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’...
2.5K
Amines to Amides: Acylation of Amines01:19

Amines to Amides: Acylation of Amines

3.0K
Various carboxylic acid derivatives (such as acid chlorides, esters, and anhydrides) can be used for the acylation of amines to yield amides. The reaction requires two equivalents of amines. The first amine molecule functions as a nucleophile and attacks the carbonyl carbon to produce a tetrahedral intermediate. This is followed by the loss of the leaving group and restoration of the C=O bond.
Next, the second equivalent of amine serves as a Brønsted base and deprotonates the quaternary...
3.0K
Amines: Introduction01:07

Amines: Introduction

4.8K
Amines are organic derivatives of ammonia. They are formed by replacing one or more ammonia protons with alkyl or aryl groups. Depending upon the number of organyl groups bonded to nitrogen, amines are classified as primary, secondary, or tertiary. Primary amines have one organyl group attached to the nitrogen atom, while secondary and tertiary amines have two and three organyl groups attached to the nitrogen atom, respectively.
4.8K
Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

3.9K
In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
3.9K
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

1.8K
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
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Updated: May 5, 2026

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
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Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

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d-amino acids: new functional insights.

Loredano Pollegioni1, Natasa Kustrimovic1, Luciano Piubelli1

  • 1The Protein Factory 2.0 Laboratory, Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.

The FEBS Journal
|March 27, 2025
PubMed
Summary

D-amino acids (d-AAs), once considered unnatural, are now recognized as vital signaling molecules in eukaryotes. Recent research highlights their diverse roles in health and disease, including as potential biomarkers.

Keywords:
d‐aspartated‐cysteined‐enantiomersd‐serinebiomarkerssignaling

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • D-amino acids (d-AAs) were historically deemed unnatural, primarily microbial, with no known eukaryotic function.
  • Advances in analytical techniques have revealed the presence of both free and peptide-bound d-AAs in higher organisms.
  • The discovery of serine racemase in mammals confirmed endogenous synthesis of d-AAs.

Purpose of the Study:

  • To review novel findings on the physiological roles of d-AAs across diverse organisms.
  • To explore the involvement of d-AAs in various pathological conditions and their potential as biomarkers.
  • To highlight the therapeutic potential of understanding d-AA metabolism and function.

Main Methods:

  • Utilized the latest analytical techniques to detect and quantify d-AAs.
  • Reviewed recent scientific literature focusing on d-AA physiological and pathological roles.
  • Integrated findings from studies across various biological systems, from plants to humans.

Main Results:

  • D-amino acids, including d-serine, d-aspartate, d-alanine, and d-cysteine, function as critical signaling molecules in the brain and endocrine system.
  • D-AAs are implicated in a wide spectrum of conditions such as neurological disorders, cancer, inflammation, immune regulation, kidney disease, and diabetes.
  • Blood and urine levels of d-AAs show promise as early biomarkers for Alzheimer's disease, schizophrenia, and chronic kidney disease.

Conclusions:

  • D-amino acids play versatile and significant roles in mammalian physiology and pathophysiology.
  • The identification of d-AAs as signaling molecules and potential biomarkers opens new avenues for disease diagnosis.
  • Targeting d-AA pathways offers promising therapeutic strategies for various human diseases.