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N-acetyl-L-glutamic acid

A J Dobson¹, R E Gerkin

¹Department of Chemistry, Ohio State University, Columbus 43210, USA.

Acta Crystallographica. Section C, Crystal Structure Communications

|January 15, 1997

Summary

This summary is machine-generated.

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N-acetyl-L-glutamic acid exhibits a unique crystal structure with six hydrogen bonds per molecule. Its carbon chain conformation is trans, differing from other L-glutamic acid forms.

Area of Science:

Biochemistry
Crystallography
Molecular Biology

Background:

N-acetyl-L-glutamic acid is a vital metabolite involved in nitrogen metabolism and the urea cycle.
Understanding its molecular structure is crucial for comprehending its biological functions and interactions.

Purpose of the Study:

To elucidate the detailed crystal structure of N-acetyl-L-glutamic acid.
To characterize the hydrogen bonding network and conformational properties.

Main Methods:

Single-crystal X-ray diffraction analysis was employed to determine the molecular structure.
Analysis of hydrogen bond donors and acceptors was performed.

Main Results:

Each molecule forms six hydrogen bonds, connecting to four other molecules.

Related Experiment Videos

An intramolecular hydrogen bond exists between the N atom and a carboxyl O atom.

The carbon chain conformation around the C3-C4 bond is trans, similar to L-glutamic acid hydrochloride.

Conclusions:

The determined crystal structure provides insights into the intermolecular interactions of N-acetyl-L-glutamic acid.
The trans conformation is a key feature distinguishing it from other L-glutamic acid derivatives.