Backbone NMR assignment of a hypothetical protein MJ0754 from Methanococcus jannaschii DSM 2661

2011 ◽  
Vol 2 (2) ◽  
pp. 46-51
Author(s):  
Eun Hye Lee ◽  
Kyoung-Seok Ryu ◽  
Kyungmin Kim ◽  
Young Ho Jeon ◽  
Kwang Yeon Hwang ◽  
...  
Keyword(s):  
Nmr Assignment ◽  
Hypothetical Protein ◽  
Methanococcus Jannaschii

scholarly journals Letter to the Editor: NMR assignment of the hypothetical protein HI0004 from Haemophilus influenzae – a putative essential gene product

2004 ◽  
Vol 29 (1) ◽  
pp. 101-102 ◽  
Author(s):  
Deok Cheon Yeh ◽  
James F. Parsons ◽  
Lisa M. Parsons ◽  
Fang Liu ◽  
Edward Eisenstein ◽  
...  
Keyword(s):  
Haemophilus Influenzae ◽  
Gene Product ◽  
Nmr Assignment ◽  
Essential Gene ◽  
Hypothetical Protein ◽  
Letter To The Editor

NMR assignment of a KlbA intein precursor from Methanococcus jannaschii

2007 ◽  
Vol 1 (1) ◽  
pp. 19-21 ◽  
Author(s):  
Margaret A. Johnson ◽  
Maurice W. Southworth ◽  
Francine B. Perler ◽  
Kurt Wüthrich
Keyword(s):  
Nmr Assignment ◽  
Methanococcus Jannaschii

Structural insights into the metal binding properties of hypothetical protein MJ0754 from Methanococcus jannaschii

2011 ◽  
Vol 79 (7) ◽  
pp. 2358-2363
Author(s):  
Eun Hye Lee ◽  
Hyun Sook Kim ◽  
Hye-Yeon Kim ◽  
Young Ho Jeon ◽  
Kwang Yeon Hwang
Keyword(s):  
Metal Binding ◽  
Hypothetical Protein ◽  
Methanococcus Jannaschii ◽  
Binding Properties ◽  
Structural Insights

scholarly journals Isolation of a Gene Responsible for the Oxidation oftrans-Anethole topara-Anisaldehyde by Pseudomonas putida JYR-1 and Its Expression in Escherichia coli

2012 ◽  
Vol 78 (15) ◽  
pp. 5238-5246 ◽  
Author(s):  
Dongfei Han ◽  
Ji-Young Ryu ◽  
Robert A. Kanaly ◽  
Hor-Gil Hur
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Putida ◽  
Hypothetical Protein ◽  
Aldehyde Group ◽  
Agrobacterium Vitis ◽  
T7 Promoter ◽  
Content Type ◽  
E Coli ◽  
Cell Extracts ◽  
Isoeugenol Monooxygenase

ABSTRACTA plasmid, pTA163, inEscherichia colicontained an approximately 34-kb gene fragment fromPseudomonas putidaJYR-1 that included the genes responsible for the metabolism oftrans-anethole to protocatechuic acid. Three Tn5-disrupted open reading frame 10 (ORF 10) mutants of plasmid pTA163 lost their abilities to catalyzetrans-anethole. Heterologously expressed ORF 10 (1,047 nucleotides [nt]) under a T7 promoter inE. colicatalyzed oxidative cleavage of a propenyl group oftrans-anethole to an aldehyde group, resulting in the production ofpara-anisaldehyde, and this gene was designatedtao(trans-anetholeoxygenase). The deduced amino acid sequence of TAO had the highest identity (34%) to a hypothetical protein ofAgrobacterium vitisS4 and likely contained a flavin-binding site. Preferred incorporation of an oxygen molecule from water intop-anisaldehyde using18O-labeling experiments indicated stereo preference of TAO for hydrolysis of the epoxide group. Interestingly, unlike the narrow substrate range of isoeugenol monooxygenase fromPseudomonas putidaIE27 andPseudomonas nitroreducensJin1, TAO fromP. putidaJYR-1 catalyzed isoeugenol,O-methyl isoeugenol, and isosafrole, all of which contain the 2-propenyl functional group on the aromatic ring structure. Addition of NAD(P)H to the ultrafiltered cell extracts ofE. coli(pTA163) increased the activity of TAO. Due to the relaxed substrate range of TAO, it may be utilized for the production of various fragrance compounds from plant phenylpropanoids in the future.

scholarly journals Paramagnetic solid-state NMR assignment and novel chemical conversion of the aldehyde group to dihydrogen ortho ester and hemiacetal moieties in copper(ii)- and cobalt(ii)-pyridinecarboxaldehyde complexes

RSC Advances ◽  
2021 ◽  
Vol 11 (33) ◽  
pp. 20216-20231
Author(s):  
Ayelén F. Crespi ◽  
Verónica M. Sánchez ◽  
Daniel Vega ◽  
Ana L. Pérez ◽  
Carlos D. Brondino ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Nmr Assignment ◽  
Cobalt Complexes ◽  
Chemical Conversion ◽  
Aldehyde Group ◽  
Ortho Ester ◽  
Complex Chemical ◽  
Chemical Functionalization

The complex chemical functionalization of the aldehyde group was elucidated in copper and cobalt complexes for 4- and 3-pyridinecarboxaldehyde ligands.

scholarly journals Identification of the Gene Encoding Sulfopyruvate Decarboxylase, an Enzyme Involved in Biosynthesis of Coenzyme M

2000 ◽  
Vol 182 (17) ◽  
pp. 4862-4867 ◽  
Author(s):  
Marion Graupner ◽  
Huimin Xu ◽  
Robert H. White
Keyword(s):  
Escherichia Coli ◽  
Second Step ◽  
Gene Products ◽  
Methanococcus Jannaschii ◽  
Coenzyme M ◽  
Gene Encoding ◽  
Fourth Step

ABSTRACT The products of two adjacent genes in the chromosome ofMethanococcus jannaschii are similar to the amino and carboxyl halves of phosphonopyruvate decarboxylase, the enzyme that catalyzes the second step of fosfomycin biosynthesis inStreptomyces wedmorensis. These two M. jannaschii genes were recombinantly expressed inEscherichia coli, and their gene products were tested for the ability to catalyze the decarboxylation of a series of α-ketoacids. Both subunits are required to form an α6β6 dodecamer that specifically catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde. This transformation is the fourth step in the biosynthesis of coenzyme M, a crucial cofactor in methanogenesis and aliphatic alkene metabolism. The M. jannaschiisulfopyruvate decarboxylase was found to be inactivated by oxygen and reactivated by reduction with dithionite. The two subunits, designated ComD and ComE, comprise the first enzyme for the biosynthesis of coenzyme M to be described.

scholarly journals Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein

2013 ◽  
Vol 41 (9) ◽  
pp. 5127-5138 ◽  
Author(s):  
Hao-Ching Wang ◽  
Mao-Lun Wu ◽  
Tzu-Ping Ko ◽  
Andrew H.-J. Wang
Keyword(s):  
Hypothetical Protein ◽  
Hu Protein
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