Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Albert, M."'
Publikováno v:
Biochemistry. 44:15768-15773
Homoserine transacetylase catalyzes one of the required steps in the biosynthesis of methionine in fungi and several bacteria. We have determined the crystal structure of homoserine transacetylase from Haemophilus influenzae to a resolution of 1.65 A
Publikováno v:
Biochemistry. 40:5665-5673
The three-dimensional structure of the lytic transglycosylase from bacteriophage lambda, also known as bacteriophage lambda lysozyme, complexed to the hexasaccharide inhibitor, hexa-N-acetylchitohexaose, has been determined by X-ray crystallography a
Autor:
Sharlyn J. Mazur, Barbara Zajc, Laura Custer, Jane M. Sayer, Albert M. Cheh, Don R. Phillips, Donald M. Jerina, Carleen Cullinane, Vilhelm A. Bohr
Publikováno v:
Biochemistry. 38:569-581
The potent environmental carcinogen benzo[a]pyrene (BaP), following enzymatic activation to enantiomeric pairs of bay-region 7,8-diol 9,10-epoxides (the benzylic 7-hydroxyl group and epoxide oxygen are cis for DE-1 diastereomers and trans for DE-2 di
Publikováno v:
Biochemistry. 35:9309-9313
Spectroscopic evidence of a DNA bend in solution is presented by analyzing model 15-mer duplexes spin-labeled with the five-atom-tethered nitroxide DUAP located in the major groove. Three 15-mers containing AATT with DUAP enzymatically incorporated i
Autor:
L. Aravind, Eric D. Brown, Denis M. Daigle, Laura Rossi, Eugene V. Koonin, Albert M. Berghuis
Publikováno v:
Biochemistry. 41(37)
The Escherichia coli protein YjeQ represents a protein family whose members are broadly conserved in bacteria and have been shown to be indispensable to the growth of E. coli and Bacillus subtilis [Arigoni, F., et al. (1998) Nat. Biotechnol. 16, 851]
Publikováno v:
Biochemistry. 41(22)
The aminoglycoside antibiotic resistance kinases (APHs) and the Ser/Thr/Tyr protein kinases share structural and functional homology but very little primary sequence conservation (
Publikováno v:
Biochemistry. 40(30)
3',5"-Aminoglycoside phosphotransferase type IIIa [APH(3')-IIIa] is a bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics while exhibiting striking homology to eukaryotic protein kinases (ePK). The structures of APH(3')-
Publikováno v:
Biochemistry. 35(33)
The influence of mutations in two conserved regions of yeast iso-1-cytochrome c believed to be critical to the mechanism of cytochrome c electron transfer reactions has been investigated. The variants Asn52Ala, Tyr67Phe, Ile75Met, and Thr78Gly involv
Autor:
Albert M. Bobst, Robert S. Keyes
Publikováno v:
Biochemistry. 34(28)
DNA motions consist of several components which couple, making their investigation difficult. This study describes an approach for obtaining dynamical information by EPR when spin-labeled nucleic acids are examined. The analysis is accomplished by im
Publikováno v:
Biochemistry. 33(43)
The carcinogen (+)-(1R,2S,3R,4S)-3,4-dihydroxy-1,2-epoxy-1,2,3,4- tetrahydrobenzo[c]phenanthrene (in which the 4-OH group and epoxide oxygen are cis) was reacted with duplexes formed from self-complementary oligodeoxyribonucleotides, producing 1S or