Results 141 to 150 of about 15,817,770 (195)

Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine. [PDF]

Acta Crystallogr F Struct Biol Commun, 2015
Xu Y, Quan CS, Jin X, Jin X, Zhao J, Jin L, Kim JS, Guo J, Fan S, Ha NC.   +9 more
europepmc   +1 more source

Crystallization and preliminary X-ray diffraction analysis of the S-adenosylhomocysteine hydrolase (SAHH) from Thermotoga maritima. [PDF]

Acta Crystallogr F Struct Biol Commun, 2014
He M, Zheng Y, Huang CH, Qian G, Xiao X, Ko TP, Shao W, Guo RT.   +7 more
europepmc   +1 more source

Sulfur-Containing Amino Acids: The Conversion Process from Product to Substrate. [PDF]

Int J Mol Sci
Zheng P, Jin Y, Wei C, Xia C.
europepmc   +1 more source

A Novel Multimodal LC-MS/MS Panel for the Comprehensive Diagnosis of Neurometabolic Disorders in CSF. [PDF]

J Inherit Metab Dis
Christ S, Rossmann J, Richter S, Garbade S, Klinke G, Blau N, Hoffmann GF, Okun JG, Opladen T.   +8 more
europepmc   +1 more source

Polymorphism of S-Adenosylhomocysteine Hydrolase in Italy [PDF]

Human Heredity, 1987
S-adenosylhomocysteine hydrolase (SAHH) polymorphism has been investigated in the Italian population. Three common alleles, SAHH*1, SAHH*2 and SAHH*3, have been observed and the estimated gene frequencies are 0.968, 0.023 and 0.009, respectively. SAHH activity has been assayed in 50 healthy individuals and the mean activity was 0.043 +/- 0.017 mumol ...
CORBO, Rosa Maria, R. Palmarino, E. Schiattarella, M. A. Giannini, R. Scacchi   +4 more
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Structure and Function of S-Adenosylhomocysteine Hydrolase

Cell Biochemistry and Biophysics, 2000
In mammals, S-adenosylhomocysteine hydrolase (AdoHcyase) is the only known enzyme to catalyze the breakdown of S-adenosylhomocysteine (AdoHcy) to homocysteine and adenosine. AdoHcy is the product of all adenosylmethionine (AdoMet)-dependent biological transmethylations.
Krzysztof Kuczera, P Lynne Howell, R T Borchardt   +2 more
exaly   +3 more sources

Inactivation of S-adenosylhomocysteine hydrolase by nucleosides

BBA - Proteins and Proteomics, 1985
The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxyadenosine inactivates as potently as 9-beta-D-arabinofuranosyladenine (Ara-A).
Giulio L Cantoni, P K Chiang, Peter K Chiang   +2 more
exaly   +3 more sources