Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Sreelatha G. Reddy"'
Publikováno v:
Journal of the American Chemical Society. 121:1175-1178
The first six cytoplasmic intermediates of murein biosynthesis (2−7) have been prepared in high yield (>60%) and at preparative scale (10−100 mg) using purified enzymes of the murein biosynthetic p...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89ee9b0edb778a03d52a7c02e40a82a7
https://doi.org/10.1021/ja983850b
https://doi.org/10.1021/ja983850b
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 8:1643-1648
A series of transition-state analog inhibitors of the D-glutamic acid-adding enzyme (MurD) of bacterial peptidoglycan biosynthesis has been synthesized and evaluated for inhibition of the E. coli enzyme.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::083f7685d89b797885d1239f3dd17964
https://doi.org/10.1016/s0960-894x(98)00285-6
https://doi.org/10.1016/s0960-894x(98)00285-6
Autor:
Maurizio Cirilli, Giovanna Scapin, John C. Vederas, Yong Gao, John S. Blanchard, Sreelatha G. Reddy
Publikováno v:
Biochemistry. 37:3278-3285
The three-dimensional structures of Corynebacterium glutamicum diaminopimelate dehydrogenase as a binary complex with the substrate meso-diaminopimelate (meso-DAP) and a ternary complex with NADP+ and an isoxazoline inhibitor [Abbot, S.D., Lane-Bell,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2399a0679de1978b30f1d1c7db2f64b5
https://doi.org/10.1021/bi9727949
https://doi.org/10.1021/bi9727949
Publikováno v:
Biochemistry. 36:15081-15088
Dihydrodipicolinate reductase catalyzes the NAD(P)H-dependent reduction of the alpha,beta-unsaturated cyclic imine dihydrodipicolinate to form the cyclic imine tetrahydrodipicolinate. The enzyme is a component of the biosynthetic pathway that leads t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c928611c1f73deb11457288118be51cd
https://doi.org/10.1021/bi9719915
https://doi.org/10.1021/bi9719915
Publikováno v:
Biochemistry. 35:13540-13551
Diaminopimelate dehydrogenase catalyzes the NADPH-dependent reduction of ammonia and L-2-amino-6-ketopimelate to form meso-diaminopimelate, the direct precursor of L-lysine in the bacterial lysine biosynthetic pathway. Since mammals lack this metabol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd8a0c240b6427e80f260d284e68c231
https://doi.org/10.1021/bi961628i
https://doi.org/10.1021/bi961628i
Publikováno v:
ChemInform. 29
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bfe54ceda55c61c18c737b2c36eada6a
https://doi.org/10.1002/chin.199843258
https://doi.org/10.1002/chin.199843258
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 25:514-516
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2429fda1070eb8e8f1fa1714cf94d40
https://doi.org/10.1002/(sici)1097-0134(199608)25:4<514::aid-prot12>3.0.co
https://doi.org/10.1002/(sici)1097-0134(199608)25:4<514::aid-prot12>3.0.co
Autor:
Jack Peisach, Richard S. Magliozzo, Kenny K. Wong, John W. Kozarich, Camran V. Parast, Sreelatha G. Reddy
Publikováno v:
Biochemistry. 37(2)
We here report EPR studies that provide evidence for radical intermediates generated from the glycyl radical of activated pyruvate formate-lyase (PFL) during the process of oxygen-dependent enzyme inactivation, radical quenching, and protein fragment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52dffcf37c05d58d800a29a05e701fe8
https://pubmed.ncbi.nlm.nih.gov/9425077
https://pubmed.ncbi.nlm.nih.gov/9425077
Publikováno v:
Biochemistry. 35(41)
E. coli dihydrodipicolinate reductase exhibits unusual nucleotide specificity, with NADH being kinetically twice as effective as NADPH as a reductant as evidenced by their relative V/K values. To investigate the nature of the interactions which deter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03c0072c5a22dbfb9f0bf6dda1bbfca1
https://pubmed.ncbi.nlm.nih.gov/8873595
https://pubmed.ncbi.nlm.nih.gov/8873595
Publikováno v:
Proteins. 25(4)
The gene encoding the meso-diaminopimelate dehydrogenase (DAPDH) from Corynebacterium glutamicum was over-expressed and purified to homogeneity. Crystals of the binary DAPDH-NADP+ complex were obtained from solutions of polyethylene glycol 8000, 100
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81d2acc146e78ca60303bd1e9b45c53e
https://pubmed.ncbi.nlm.nih.gov/8865347
https://pubmed.ncbi.nlm.nih.gov/8865347