Marilyn D. YoderLab Web Page |
Associate Professor
Division of Cell Biology and Biophysics School of Biological Science University of Missouri-Kansas City |
| B.S. | Nutrition | University of Kentucky |
| Ph.D. | Biochemistry | University of California, Riverside |
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Pectate
Lyases Pectate lyases are a family of proteins secreted by bacterial and fungal plant pathogens that degrade the plant cell wall and middle lamella. The enzymes cleave the glycosidic bond of pectate polymers by a calcium dependent beta-elimination mechanism. We are currently focusing on pectate lyase members from the Erwinia chrysanthemi soft-rot plant pathogens.
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PolygalacturonasesPolygalacturonases are functionally and structurally related to pectate lyases, although they share no detectable amino acid sequence similarity. These enzymes cleave the glycosidic bond of pectate polymers by a hydrolytic mechanism. Pectate lyases and polygalacturonases cleave the same substrate but by different mechanisms, thereby providing a benefical system to study structural requirements for these two enzymatic mechanisms.
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Phosphatidylinositol
Transfer Protein (PITP) PITPs are ubiqutous eukaryotic proteins involved in several signal transduction activities. The protein binds one molecule of either phoshatidylinositol or phosphatidylcholine. It's hallmark characteristic is the ability to exchange a protein bound phospholipid with one in a cellular membrane. The three-dimensional structure of the alpha isoform bound to phosphatidylcholine revealed a lipid binding domain (in blue) that is structurally similar to STaRT domain proteins.
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| Mailing Adrdress: | ||
| School of Biological Sciences | Phone (office): 1-816-235-1986 | |
| University of Missouri-Kansas City | Phone (lab): 1-816-235-2571 | |
| 5007 Rockhill Rd. | Fax: 1-816-235-1503 | |
| Kansas City, MO 64110-2499 | yoderm@umkc.edu |