AN AROMATIC AMINO ACID TRANSAMINASE FROM MUNG BEAN

A transaminase has been isolated and purified from young mung bean plants (Phaseolus aureus Roxb.). The enzyme catalyzes the transamination of phenylalanine in the presence of α-ketoglutarate with the production of equimolar amounts of phenylpyruvate and glutamate. Tyrosine and tryptophan also serve as substrates, and relative rate measurements indicate that only one enzyme is involved. In addition to α-ketoglutarate the enzyme also utilizes pyruvate, and to some extent glyoxylate and oxaloacetate as amino acceptors. The enzyme is stable in solution at 0–4 °C for several weeks, and acetone powders of the young plants stored at 0–4 °C retained their activity for several months. The enzyme is inhibited by precipitation with ammonium sulphate, and the activity is lost after freezing.

Download Full-text

The amino acid sequence of Phaseolus aureus L. (mung-bean) cytochrome c

Biochemical Journal ◽

10.1042/bj1170183 ◽

1970 ◽

Vol 117 (1) ◽

pp. 183-192 ◽

Cited By ~ 35

Author(s):

E. W. Thompson ◽

M. V. Laycock ◽

J. A. M. Ramshaw ◽

D. Boulter

Keyword(s):

Amino Acid ◽

Cytochrome C ◽

Amino Acid Sequence ◽

Mung Bean ◽

Wheat Germ ◽

Amino Acid Residues ◽

Phaseolus Aureus ◽

Single Polypeptide Chain ◽

Cytochromes C ◽

Lysine Residues

The amino acid sequence of Phaseolus aureus L. (mung-bean) cytochrome c has been determined. The molecule consists of a single polypeptide chain of 111 amino acid residues and is homologous with other mitochondrial cytochromes c. Comparison with the amino acid sequence of wheat-germ cytochrome c (Stevens, Glazer & Smith, 1967) shows 14 differences. On alignment with mammalian cytochromes c, mung-bean cytochrome c has an N-acetylated ‘tail’ of eight amino acid residues similar to that found in wheat-germ cytochrome c. Of the 22 positions in wheat-germ cytochrome c that contain amino acid residues unique to these positions, 20 were found to contain the same ones in mung-bean cytochrome c. The ∈-N-trimethyl-lysine residues reported for wheat-germ cytochrome c (Delange, Glazer & Smith, 1969) in positions 72 and 86 were also found in these positions in mung-bean cytochrome c. The sequence was determined from 3μmol, by using chymotryptic and tryptic peptides which were analysed by the ‘dansyl’–Edman method (Gray & Hartley, 1963a), with confirmation by amino acid analysis.

Download Full-text

Partial purification and characterisation of an aromatic amino acid aminotransferase from mung bean (Vigna radiata L. Wilczek)

Planta ◽

10.1007/bf01258682 ◽

1997 ◽

Vol 201 (1) ◽

pp. 71-77 ◽

Cited By ~ 9

Author(s):

R. M. Simpson ◽

H. M. Nonhebel ◽

D. L. Christie

Keyword(s):

Amino Acid ◽

Vigna Radiata ◽

Mung Bean ◽

Aromatic Amino Acid ◽

Partial Purification ◽

Aromatic Amino Acid Aminotransferase

Download Full-text

Predicting the Strength of Stacking Interactions Between Heterocycles and Aromatic Amino Acid Side Chains

10.26434/chemrxiv.7628939.v2 ◽

2019 ◽

Author(s):

Andrea N. Bootsma ◽

Analise C. Doney ◽

Steven Wheeler

Keyword(s):

Amino Acid ◽

Binding Sites ◽

Aromatic Amino Acid ◽

Aromatic Amino Acids ◽

Biologically Active ◽

Side Chains ◽

Stacking Interactions ◽

Inhibitor Binding ◽

Protein Binding Sites ◽

Amino Acid Side Chains

<p>Despite the ubiquity of stacking interactions between heterocycles and aromatic amino acids in biological systems, our ability to predict their strength, even qualitatively, is limited. Based on rigorous <i>ab initio</i> data, we have devised a simple predictive model of the strength of stacking interactions between heterocycles commonly found in biologically active molecules and the amino acid side chains Phe, Tyr, and Trp. This model provides rapid predictions of the stacking ability of a given heterocycle based on readily-computed heterocycle descriptors. We show that the values of these descriptors, and therefore the strength of stacking interactions with aromatic amino acid side chains, follow simple predictable trends and can be modulated by changing the number and distribution of heteroatoms within the heterocycle. This provides a simple conceptual model for understanding stacking interactions in protein binding sites and optimizing inhibitor binding in drug design.</p>

Download Full-text

Urinary Metabolomics Reveals Alterations of Aromatic Amino Acid Metabolism of Alzheimer's Disease in the Transgenic CRND8 Mice

Current Alzheimer Research ◽

10.2174/1567205013666160129095340 ◽

2016 ◽

Vol 13 (7) ◽

pp. 764-776 ◽

Cited By ~ 14

Author(s):

Zhi Tang ◽

Liangfeng Liu ◽

Yongle Li ◽

Jiyang Dong ◽

Min Li ◽

...

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

Amino Acid ◽

Aromatic Amino Acid ◽

Amino Acid Metabolism ◽

Acid Metabolism ◽

Aromatic Amino Acid Metabolism

Download Full-text

Self-assembling behaviour of a modified aromatic amino acid in competitive medium

Soft Matter ◽

10.1039/d0sm00584c ◽

2020 ◽

Vol 16 (28) ◽

pp. 6599-6607 ◽

Cited By ~ 1

Author(s):

Pijush Singh ◽

Souvik Misra ◽

Nayim Sepay ◽

Sanjoy Mondal ◽

Debes Ray ◽

...

Keyword(s):

Amino Acid ◽

Self Assembly ◽

Aromatic Amino Acid ◽

Photophysical Properties ◽

Solvent Mixture ◽

The Self ◽

Solvent Ratio ◽

Self Assembling

The self-assembly and photophysical properties of 4-nitrophenylalanine (4NP) are changed with the alteration of solvent and final self-assembly state of 4NP in competitive solvent mixture and are dictated by the solvent ratio.

Download Full-text