N-terminal amino acid sequence of Brevibacterium sp. R312 wide-spectrum amidase.

Appl Microbiol Biotechnol

Chaire de Microbiologie Industrielle et de Génétique des Microorganismes, Ecole Nationale Supérieure Agronomique de Montpellier, France.

Published: November 1991

A wide-spectrum amidase from Brevibacterium sp. R312 was partially purified. The enzyme subunit was purified by reversed phase HPLC and the N-terminal amino acid sequence was found to be identical to that of Pseudomonas aeruginosa aliphatic amidase.

Download full-text PDF

Source
http://dx.doi.org/10.1007/BF00164420DOI Listing

Publication Analysis

Top Keywords

n-terminal amino
8
amino acid
8
acid sequence
8
brevibacterium r312
8
wide-spectrum amidase
8
sequence brevibacterium
4
r312 wide-spectrum
4
amidase wide-spectrum
4
amidase brevibacterium
4
r312 partially
4

Similar Publications

Discovery of an Enzyme-Activated Fluorogenic Probe for Profiling of Acylaminoacyl-Peptide Hydrolase.

Anal Chem

January 2025

Department of Laboratory Medicine, School of Medicine, Yangtze University, Jingzhou 434023, P.R. China.

Acylaminoacyl-peptide hydrolase (APEH), a serine peptidase that belongs to the prolyl oligopeptidase (POP) family, catalyzes removal of N-terminal acetylated amino acid residues from peptides. As a key regulator of protein N-terminal acetylation, APEH was involved in many important physiological processes while its aberrant expression was correlated with progression of various diseases such as inflammation, diabetics, Alzheimer's disease (AD), and cancers. However, while emerging attention has been attracted in APEH-related disease diagnosis and drug discovery, the mechanisms behind APEH and related disease progression are still unclear; thus, further investigating the physiological role and function of APEH is of great importance.

View Article and Find Full Text PDF

The COP9 signalosome (CSN) is a highly conserved multi-subunit protein complex, with CSN1 being its largest and most conserved subunit. The N-terminal function of CSN1 plays a pivotal and intricate role in plant photomorphogenesis and seedling development. Moreover, CSN is essential for far-red light-mediated photomorphogenesis in seedlings, but the function of OsCSN1 in seedling growth and development under far-red light conditions has not been determined.

View Article and Find Full Text PDF

Cryo-EM structure and regulation of human NAD kinase.

Sci Adv

January 2025

Atelier de Biologie Chimie Informatique Structurale, Centre de Biologie Structurale, Univ Montpellier, CNRS, INSERM, 29 rue de Navacelles, 34090 Montpellier, France.

Reduced nicotinamide adenine dinucleotide phosphate (NADPH) is a crucial reducing cofactor for reductive biosynthesis and protection from oxidative stress. To fulfill their heightened anabolic and reductive power demands, cancer cells must boost their NADPH production. Progrowth and mitogenic protein kinases promote the activity of cytosolic NAD kinase (NADK), which produces NADP, a limiting NADPH precursor.

View Article and Find Full Text PDF

Type 2 diabetes mellitus (T2DM) and obesity are critical global health issues with rising incidence rates. Glucagon-like peptide-1 (GLP-1) analogues have emerged as effective treatments due to their ability to regulate blood glucose levels and gastric emptying through central nervous signals involving hypothalamic receptors, such as leptin. To address the short plasma half-life of native GLP-1, a C-16 fatty acid was conjugated to lysine in the GLP-1 analogue sequence to enhance its longevity.

View Article and Find Full Text PDF

The N17 domain of huntingtin as a multifaceted player in Huntington's disease.

Front Mol Biosci

January 2025

Center for Biomolecular and Cellular Structure, Institute for Basic Science, Daejeon, Republic of Korea.

Huntington's disease (HD) is primarily caused by the aberrant aggregation of the N-terminal exon 1 fragment of mutant huntingtin protein (mHttex1) with expanded polyglutamine (polyQ) repeats in neurons. The first 17 amino acids of the N-terminus of Httex1 (N17 domain) immediately preceding the polyQ repeat domain are evolutionarily conserved across vertebrates and play multifaceted roles in the pathogenesis of HD. Due to its amphipathic helical properties, the N17 domain, both alone and when membrane-associated, promotes mHttEx1 aggregation.

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!