Structure, function and substrate preferences of archaeal S-adenosyl-l-homocysteine hydrolases
LH Koeppl, D Popadić, R Saleem-Batcha… - Communications …, 2024 - nature.com
S-Adenosyl-l-homocysteine hydrolase (SAHH) reversibly cleaves S-adenosyl-l-
homocysteine, the product of S-adenosyl-l-methionine-dependent methylation reactions …
homocysteine, the product of S-adenosyl-l-methionine-dependent methylation reactions …
Purification, Gene Cloning, and Characterization of a Novel Halohydrin Dehalogenase from Agromyces mediolanus ZJB120203
F Xue, ZQ Liu, NW Wan, YG Zheng - Applied biochemistry and …, 2014 - Springer
A novel halohydrin dehalogenase (HHDH), catalyzing the transformation of 1, 3-dichloro-2-
propanol (1, 3-DCP) to epichlorohydrin (ECH), was purified from Agromyces mediolanus …
propanol (1, 3-DCP) to epichlorohydrin (ECH), was purified from Agromyces mediolanus …
S-adenosyl-L-homocysteine hydrolase from a hyperthermophile (Thermotoga maritima) is expressed in Escherichia coli in inactive form–Biochemical and structural …
K Brzezinski, J Czyrko, J Sliwiak… - International journal of …, 2017 - Elsevier
Thermotoga maritima is a hyperthermophilic bacterium but its genome encodes a number of
archaeal proteins including S-adenosyl-L-homocysteine hydrolase (SAHase), which …
archaeal proteins including S-adenosyl-L-homocysteine hydrolase (SAHase), which …
Crystal structures of S-adenosylhomocysteine hydrolase from the thermophilic bacterium Thermotoga maritima
Y Zheng, CC Chen, TP Ko, X Xiao, Y Yang… - Journal of Structural …, 2015 - Elsevier
S-adenosylhomocysteine (SAH) hydrolase catalyzes the reversible hydrolysis of SAH into
adenosine and homocysteine by using NAD+ as a cofactor. The enzyme from Thermotoga …
adenosine and homocysteine by using NAD+ as a cofactor. The enzyme from Thermotoga …
NAD+ enhances the activity and thermostability of S-adenosyl-L-homocysteine hydrolase from Pyrococcus horikoshii OT3
R Iwasaki, T Bito, A Ishihara… - Bioscience …, 2023 - academic.oup.com
ABSTRACT S-Adenosyl-L-methionine (SAM) and S-adenosyl-L-homocysteine (SAH) are
important biochemical intermediates. SAM is the major methyl donor for diverse methylation …
important biochemical intermediates. SAM is the major methyl donor for diverse methylation …
A thermostable S-adenosylhomocysteine hydrolase from Thermotoga maritima: properties and its application on S-adenosylhomocysteine production with enzymatic …
G Qian, C Chen, R Zhou, Y He, W Shao - Enzyme and microbial technology, 2014 - Elsevier
S-adenosylhomocysteine (SAH) is an effective sedative, a good sleep modulator, and a new
anticonvulsant. SAH can be synthesized from adenosine and homocysteine by using …
anticonvulsant. SAH can be synthesized from adenosine and homocysteine by using …
Archaeal S-adenosyl-l-homocysteine hydrolases: structure, function and substrate preferences
D Popadić, R Saleem-Batcha, LH Köppl, P Germer… - bioRxiv, 2023 - biorxiv.org
S-Adenosyl-l-homocysteine hydrolase (SAHH) reversibly cleaves S-adenosyl-l-
homocysteine (SAH), the product of S-adenosyl-l-methionine (SAM)-dependent methylation …
homocysteine (SAH), the product of S-adenosyl-l-methionine (SAM)-dependent methylation …
Functional Studies Of 5-Carboxyaminoimidazole Ribonucleotide Synthetase And Mutase From Thermotoga Maritima
M Zhao - 2014 - digitalcommons.wayne.edu
De novo purine biosynthesis is divergent depending upon the organism. In bacteria, yeasts
and plants, 5-aminoimidazole ribonucleotide (AIR) is converted to 4-carboxyaminoimidazole …
and plants, 5-aminoimidazole ribonucleotide (AIR) is converted to 4-carboxyaminoimidazole …
Crystallization and preliminary X-ray diffraction analysis of the S-adenosylhomocysteine hydrolase (SAHH) from Thermotoga maritima
M He, Y Zheng, CH Huang, G Qian, X Xiao… - … Section F: Structural …, 2014 - journals.iucr.org
S-Adenosylhomocysteine hydrolase (SAHH) catalyzes the reversible conversion of S-
adenosylhomocysteine into adenosine and homocysteine. The SAHH from Thermotoga …
adenosylhomocysteine into adenosine and homocysteine. The SAHH from Thermotoga …
재조합고온성Xylose Isomerase 처리에의한사포닌및푸코이단의암세포생육저해활성비교
이동근， 박성환， 이상현 - KSBB Journal, 2013 - dbpia.co.kr
호열성 진정세균인 Thermotoga maritima 의 xylose isomerase 유전자를 대장균을 이용하여
클로닝하고 재조합 발현시켰다. 재조합 효소의 최적활성은 90℃ 와 pH 8.0 에서 관찰되었다 …
클로닝하고 재조합 발현시켰다. 재조합 효소의 최적활성은 90℃ 와 pH 8.0 에서 관찰되었다 …