Sequence specific resonance assignments have been obtained for (1)H, (13)C and (15)N nuclei of the 21 kDa (188 residues long) glutamine amido transferase subunit of guanosine monophosphate synthetase from Methanocaldococcus jannaschii. From an analysis of (1)H and (13)C(α), (13)C(β) secondary chemical shifts, (3) JH(N)H(α) scalar coupling constants and sequential, short and medium range (1)H-(1)H NOEs, it was deduced that the glutamine amido transferase subunit has eleven strands and five helices as the major secondary structural elements in its tertiary structure.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s12104-011-9354-xDOI Listing

Publication Analysis

Top Keywords

glutamine amido
12
amido transferase
12
transferase subunit
12
13c 15n
8
monophosphate synthetase
8
synthetase methanocaldococcus
8
methanocaldococcus jannaschii
8
15n assignment
4
assignment secondary
4
secondary structure
4

Similar Publications

S basic leucine zipper transcription factors shape plant architecture by controlling C/N partitioning to apical and lateral organs.

Proc Natl Acad Sci U S A

February 2024

Department of Pharmaceutical Biology, Faculty of Biology, Biocenter, Julius-von-Sachs-Institute, Julius-Maximilians-Universität Würzburg, Würzburg 97082, Germany.

Plants tightly control growth of their lateral organs, which led to the concept of apical dominance. However, outgrowth of the dormant lateral primordia is sensitive to the plant's nutritional status, resulting in an immense plasticity in plant architecture. While the impact of hormonal regulation on apical dominance is well characterized, the prime importance of sugar signaling to unleash lateral organ formation has just recently emerged.

View Article and Find Full Text PDF

The hemibiotrophic bacterial pathogen Pseudomonas syringae infects a range of plant species and causes enormous economic losses. Auxin and WRKY transcription factors play crucial roles in plant responses to P. syringae, but their functional relationship in plant immunity remains unclear.

View Article and Find Full Text PDF

Glutamine (Gln) is the first amino acid synthesized in nitrogen (N) assimilation in plants. Gln synthetase (GS), converting glutamate (Glu) and NH4+ into Gln at the expense of ATP, is one of the oldest enzymes in all life domains. Plants have multiple GS isoenzymes that work individually or cooperatively to ensure that the Gln supply is sufficient for plant growth and development under various conditions.

View Article and Find Full Text PDF

L-Glutamine-, peptidyl- and protein-glutaminases: structural features and applications in the food industry.

World J Microbiol Biotechnol

August 2022

Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) - Instituto de Ciencia y Tecnología de los Alimentos de Entre Ríos (ICTAER), Monseñor Tavella 1450 (E3202 BCJ), Concordia, Entre Ríos, Argentina.

L-Glutaminases are enzymes that catalyze the cleavage of the gamma-amido bond of L-glutamine residues, producing ammonia and L-glutamate. These enzymes have several applications in food and pharmaceutical industries. However, the L-glutaminases that hydrolyze free L-glutamine (L-glutamine glutaminases, EC 3.

View Article and Find Full Text PDF

We examined the ability of two human cytosolic transaminases, aspartate aminotransferase (GOT1) and alanine aminotransferase (GPT), to transform their preferred substrates whilst discriminating against similar metabolites. This offers an opportunity to survey our current understanding of enzyme selectivity and specificity in a biological context. Substrate selectivity can be quantitated based on the ratio of the / values for two alternative substrates (the 'discrimination index').

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!