Zobrazeno 1 - 10
of 300
pro vyhledávání: '"A S, Mildvan"'
Publikováno v:
Biochemistry. 46:12833-12843
Methionine aminopeptidases (MetAP) are responsible for the proteolytic removal of the initiator methionine from nascent proteins. This processing permits multiple posttranslational modifications and protein turnover. We have cloned, expressed in Esch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87b6511835143c97982a31453648108e
https://doi.org/10.1021/bi701127x
https://doi.org/10.1021/bi701127x
Publikováno v:
Biochemistry. 45:11290-11303
GDP-mannose hydrolase catalyzes the hydrolysis with inversion of GDP-{alpha}-D-hexose to GDP and {beta}-D-hexose by nucleophilic substitution by water at C1 of the sugar. Two new crystal structures (free enzyme and enzyme-substrate complex), NMR, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1460b78d3940af2529b5b92240017752
https://doi.org/10.1021/bi061239g
https://doi.org/10.1021/bi061239g
Autor:
Albert S. Mildvan, L.M. Amzel, Sandra B. Gabelli, Stephen G. Withers, Patricia M. Legler, Zuyong Xia, Mario A. Bianchet, Luke L. Lairson, M.R. Balfour, Hugo F. Azurmendi
Publikováno v:
Journal of Molecular Structure. 790:160-167
GDP-mannose mannosyl hydrolase (GDPMH) from E. coli catalyzes the hydrolysis of GDP-α- d -sugars to GDP and β- d -sugars by nucleophilic substitution with inversion at the anomeric C1 of the sugar, with general base catalysis by His-124. The 1.3 A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b17a3b5eba0388cffa3abec6c0e95e9
https://doi.org/10.1016/j.molstruc.2005.09.024
https://doi.org/10.1016/j.molstruc.2005.09.024
Publikováno v:
Biochemistry. 44:7725-7737
4-Oxalocrotonate tautomerase (4-OT), a homohexameric enzyme, converts the unconjugated enone, 2-oxo-4-hexenedioate (1), to the conjugated enone, 2-oxo-3-hexenedioate (3), via a dienolic intermediate, 2-hydroxymuconate (2). Pro-1 serves as the general
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed0670e7badb98a1b2b9572c64c7ef09
https://doi.org/10.1021/bi0502590
https://doi.org/10.1021/bi0502590
Autor:
Albert S. Mildvan
Publikováno v:
Biochemistry. 43:14517-14520
The quantitative effect of a second damaging mutation on a mutated enzyme may be additive, partially additive, synergistic, antagonistic, or absent, in the double mutant. Each of these five possible types of interactions has its own mechanistic expla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f245e6a398315edd070178d606cd8b9e
https://doi.org/10.1021/bi048052e
https://doi.org/10.1021/bi048052e
Publikováno v:
Journal of Molecular Structure. 700:247-254
The MutT pyrophosphohydrolase from E. coli (129 residues) catalyzes the hydrolysis of nucleoside triphosphates (NTP), including 8-oxo-dGTP, by substitution at Pβ, to yield NMP and pyrophosphate. The product, 8-oxo-dGMP is an unusually tight binding,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f2be3e53c5729878e2a5be0974136e4
https://doi.org/10.1016/j.molstruc.2003.12.060
https://doi.org/10.1016/j.molstruc.2003.12.060
Autor:
Michael A. Massiah, Albert S. Mildvan, Susan C. Wang, Hugo F. Azurmendi, Gerrit J. Poelarends, Christian P. Whitman
Publikováno v:
Biochemistry. 43:4082-4091
trans-3-Chloroacrylic acid dehalogenase (CaaD) converts trans-3-chloroacrylic acid to malonate semialdehyde by the addition of H(2)O to the C-2, C-3 double bond, followed by the loss of HCl from the C-3 position. Sequence similarity between CaaD, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbdbd0bcfdd0c994233cdc8d75297e21
https://doi.org/10.1021/bi030241u
https://doi.org/10.1021/bi030241u
Publikováno v:
Biochemistry. 42:10140-10154
To learn the structural basis for the unusually tight binding of 8-oxo-nucleotides to the MutT pyrophosphohydrolase of Escherichia coli (129 residues), the solution structure of the MutT-Mg(2+)-8-oxo-dGMP product complex (K(D) = 52 nM) was determined
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82f5aa2079a9e1734bc7bc17aa45a7fd
https://doi.org/10.1021/bi030105p
https://doi.org/10.1021/bi030105p
Publikováno v:
Biochemistry. 41:15566-15577
The MutT enzyme from E. coli, in the presence of a divalent cation, catalyzes the hydrolysis of nucleoside- and deoxynucleoside-triphosphate (NTP) substrates by nucleophilic substitution at Pbeta, to yield a nucleotide (NMP) and PPi. The best substra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6350a429dadd02269ec76e973c2fd645
https://doi.org/10.1021/bi020552p
https://doi.org/10.1021/bi020552p
Autor:
Putta Mallikarjuna Reddy, Albert S. Mildvan, Gregory T. Marks, David H. T. Harrison, Michael A. Massiah, Carol Viragh, Ildiko M. Kovach, Thomas K. Harris
Publikováno v:
Journal of Molecular Structure. 615:163-175
The lengths of short, strong hydrogen bonds (SSHBs) on enzymes have been determined with high precision (±0.05 A) from the chemical shifts (δ), and independently from the D/H fractionation factors (φ) of the highly deshielded protons involved. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89b142b2e43bd588568cc6b0ad094d5d
https://doi.org/10.1016/s0022-2860(02)00212-0
https://doi.org/10.1016/s0022-2860(02)00212-0