Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Katherine S. Bateman"'
Publikováno v:
Journal of Medicinal Chemistry. 54:1421-1429
β-Hexosaminidases (β-hex) are a group of glycosyl hydrolase isozymes that break down neutral and sialylated glycosphingolipids in the lysosomes, thereby preventing their buildup in neuronal cells. Some mutants of β-hex have decreased folding stabi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ac3f0723b9b588f10a27c68276b3241
https://doi.org/10.1021/jm101443u
https://doi.org/10.1021/jm101443u
Autor:
Katherine S. Bateman, Stephen Anderson, Wuyuan Lu, Michael Laskowski, M. A. Qasim, Michael N.G. James
Publikováno v:
Protein Science. 9:83-94
Turkey ovomucoid third domain (OMTKY3) is a canonical inhibitor of serine proteinases. Upon complex formation, the inhibitors fully exposed P1 residue becomes fully buried in the preformed cavity of the enzyme. All 20 P1 variants of OMTKY3 have been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c54b4af54fb8958cc7cc66b92098be5f
https://doi.org/10.1110/ps.9.1.83
https://doi.org/10.1110/ps.9.1.83
Publikováno v:
Biochemistry. 41:14455-14462
Ketoacidosis affects patients who are deficient in the enzyme activity of succinyl-CoA:3-ketoacid CoA transferase (SCOT), since SCOT catalyses the activation of acetoacetate in the metabolism of ketone bodies. Thus far, structure/function analysis of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbbbaff0d5679d2596e589a9870c0b86
https://doi.org/10.1021/bi020568f
https://doi.org/10.1021/bi020568f
Autor:
Katherine S. Bateman, Jinhui Ding, Philip J. Ganz, Charles W. Saunders, Michael Laskowski, Stephen Anderson, John L. Markley, M. A. Qasim, Stephen M. Lu, Michael N. G. James, Jikui Song
Publikováno v:
Biochemistry. 38:7142-7150
Eglin c, turkey ovomucoid third domain, and bovine pancreatic trypsin inhibitor (Kunitz) are all standard mechanism, canonical protein inhibitors of serine proteinases. Each of the three belongs to a different inhibitor family. Therefore, all three h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::473a9ff8db7cf813f146f857a2a3c767
https://doi.org/10.1021/bi990265u
https://doi.org/10.1021/bi990265u
Autor:
Charles W. Saunders, Michael N. G. James, Katherine S. Bateman, Michael Laskowski, Philip J. Ganz, M. A. Qasim
Publikováno v:
Biochemistry. 36:1598-1607
Standard mechanism protein inhibitors of serine proteinases share a common mechanism of interaction with their cognate enzymes. The P1 residue of the inhibitor interacts with the enzyme in a substrate-like manner. Its side chain becomes imbedded in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9c1cbd4d6f3ad7d210b271659ff4e79
https://doi.org/10.1021/bi9620870
https://doi.org/10.1021/bi9620870
Autor:
Chang-Yub Kim, Katherine S. Bateman, Li-Wei Hung, Heungbok Kim, Craig R. Garen, Minmin Yu, Michael N.G. James, Emily Alipio Lyon, Jiang Yin, Jeff Habel
The gene product of the open reading frame Rv3340 from Mycobacterium tuberculosis is annotated as encoding a probable O-acetylhomoserine (OAH) sulfhydrylase (MetC), an enzyme that catalyzes the last step in the biosynthesis of methionine, which is an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f62579073e19a7fecca8d42cb8a5a099
https://europepmc.org/articles/PMC3151138/
https://europepmc.org/articles/PMC3151138/
Publikováno v:
Current proteinpeptide science. 12(5)
This review outlines known examples of the three-dimensional structures of protein proteinase inhibitors from plants. Three families of enzymes, serine proteinases, carboxypeptidases and cysteine proteinases, are targeted by at least a dozen inhibito
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e7d5af6d45dcec35ea40627470162c1
https://pubmed.ncbi.nlm.nih.gov/21418022
https://pubmed.ncbi.nlm.nih.gov/21418022
Publikováno v:
The Journal of biological chemistry. 285(35)
ATP-citrate lyase (ACLY) catalyzes the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, coupled with the hydrolysis of ATP. In humans, ACLY is the cytoplasmic enzyme linking energy metabolism from carbohydrates to the production of fat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25975be24b80d7761420cc645e0f7a0f
https://pubmed.ncbi.nlm.nih.gov/20558738
https://pubmed.ncbi.nlm.nih.gov/20558738
Autor:
Katherine S. Bateman, Maia M. Cherney, M. Joanne Lemieux, Michael N.G. James, Sarah J. Fischer
Rhomboid peptidases are members of a family of regulated intramembrane peptidases that cleave the transmembrane segments of integral membrane proteins. Rhomboid peptidases have been shown to play a major role in developmental processes in Drosophila
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::275848018c3b760476b0af55cd9c71c6
https://europepmc.org/articles/PMC1783385/
https://europepmc.org/articles/PMC1783385/
Autor:
Hue Anh Luu, Katherine S. Bateman, Amit Das, Charles F.B. Holmes, Maia M. Cherney, Michael N.G. James, Jason T. Maynes
Publikováno v:
The Journal of biological chemistry. 276(47)
Protein phosphatase-1 (PP1) plays a key role in dephosphorylation in numerous biological processes such as glycogen metabolism, cell cycle regulation, smooth muscle contraction, and protein synthesis. Microorganisms produce a variety of inhibitors of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::effc6fab397d086905616fd529eb7c20
https://pubmed.ncbi.nlm.nih.gov/11535607
https://pubmed.ncbi.nlm.nih.gov/11535607