Kinetic and Mutagenic Evidence for the Role of Histidine Residues in the Lycopersicon esculentum 1-Aminocyclopropane-1-carboxylic acid Oxidase
dc.contributor.author | Tayeh, Mahmoud A. | en_US |
dc.contributor.author | Howe, David L. | en_US |
dc.contributor.author | Salleh, Hamzah M. | en_US |
dc.contributor.author | Sheflyan, Galina Ya. | en_US |
dc.contributor.author | Son, Jong-Keun | en_US |
dc.contributor.author | Woodard, Ronald W. | en_US |
dc.date.accessioned | 2006-09-11T15:39:10Z | |
dc.date.available | 2006-09-11T15:39:10Z | |
dc.date.issued | 1999-01 | en_US |
dc.identifier.citation | Tayeh, Mahmoud A.; Howe, David L.; Salleh, Hamzah M.; Sheflyan, Galina Ya.; Son, Jong-Keun; Woodard, Ronald W.; (1999). "Kinetic and Mutagenic Evidence for the Role of Histidine Residues in the Lycopersicon esculentum 1-Aminocyclopropane-1-carboxylic acid Oxidase." Journal of Protein Chemistry 18(1): 55-68. <http://hdl.handle.net/2027.42/45083> | en_US |
dc.identifier.issn | 1573-4943 | en_US |
dc.identifier.issn | 0277-8033 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/45083 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=10071929&dopt=citation | en_US |
dc.description.abstract | The ACCO gene from Lycopersicon esculentum (tomato) has been cloned into the expression vector PT7-7. The highly expressed protein was recovered in the form of inclusion bodies. ACCO is inactivated by diethyl pyrocarbonate (DEPC) with a second-order rate constant of 170 M −1 min −1 . The pH–inactivation rate data imply the involvement of an amino acid residue with a p K value of 6.05. The difference UV spectrum of the the DEPC-inactivated versus native ACCO showed a single peak at 242 nm indicating the modification of histidine residues. The inactivation was reversed by the addition of hydroxylamine to the DEPC-inactivated ACCO. Substrate/cofactor protection studies indicate that both iron and ACC bind near the active site, which contains histidine residues. Four histidines of ACCO were individually mutated to alanine and glycine. H39A is catalytically active, while H177A, H177G, H211A, H211G, H234A, and H234G are basically inactive. The results indicate that histidine residues 177, 211, and 234 may serve as ligands for the active-site iron of ACCO and/or may play some important structural or catalytic role. | en_US |
dc.format.extent | 1268787 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Media | en_US |
dc.subject.other | Organic Chemistry | en_US |
dc.subject.other | Mutagenesis | en_US |
dc.subject.other | Chemical Modification | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Bioorganic Chemistry | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.subject.other | ACC Oxidase | en_US |
dc.subject.other | DEPC | en_US |
dc.subject.other | Histidine | en_US |
dc.title | Kinetic and Mutagenic Evidence for the Role of Histidine Residues in the Lycopersicon esculentum 1-Aminocyclopropane-1-carboxylic acid Oxidase | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Interdepartmental Program in Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, 48109-1065 | en_US |
dc.contributor.affiliationum | Interdepartmental Program in Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, 48109-1065 | en_US |
dc.contributor.affiliationum | Interdepartmental Program in Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, 48109-1065 | en_US |
dc.contributor.affiliationum | Interdepartmental Program in Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, 48109-1065 | en_US |
dc.contributor.affiliationum | Interdepartmental Program in Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, 48109-1065 | en_US |
dc.contributor.affiliationum | Interdepartmental Program in Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, 48109-1065 | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 10071929 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/45083/1/10930_2004_Article_409396.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1023/A:1020647400034 | en_US |
dc.identifier.source | Journal of Protein Chemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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