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Difference between revisions of "Glycoside Hydrolase Family 18"
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;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation <cite>4</cite>. | ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation <cite>4</cite>. | ||
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation <cite>2</cite>. | ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation <cite>2</cite>. | ||
− | ;First 3-D structure: | + | ;First 3-D structure: The first two 3-D structures for GH18 members were the Serratia marcescens chitinase A and the plant defence protein hevamine published "back-to-back" in ''Structure'' in 1994 <cite>Perrakis,ATVA</cite> Groups. . |
== References == | == References == | ||
<biblio> | <biblio> | ||
− | # | + | #Perrakis pmid=7704527 |
− | # | + | #ATVA1 pmid=7704528 |
+ | #AVTA2 pmid=7495789 | ||
#3 isbn=978-0-240-52118-3 | #3 isbn=978-0-240-52118-3 | ||
#4 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | #4 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] |
Revision as of 04:04, 6 October 2010
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author: ^^^Gideon Davies^^^
- Responsible Curator: ^^^Gideon Davies^^^
Glycoside Hydrolase Family GH18 | |
Clan | GH-x |
Mechanism | retaining/inverting |
Active site residues | known/not known |
CAZy DB link | |
http://www.cazy.org/fam/GH18.html |
Substrate specificities
Content is to be added here.
This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First sterochemistry determination
- Cite some reference here, with a short (1-2 senetence) explanation [1].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 senetence) explanation [4].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 senetence) explanation [2].
- First 3-D structure
- The first two 3-D structures for GH18 members were the Serratia marcescens chitinase A and the plant defence protein hevamine published "back-to-back" in Structure in 1994 [5, 6] Groups. .
References
- Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science.
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, Wilson KS, and Vorgias CE. (1994). Crystal structure of a bacterial chitinase at 2.3 A resolution. Structure. 1994;2(12):1169-80. DOI:10.1016/s0969-2126(94)00119-7 |
- Terwisscha van Scheltinga AC, Kalk KH, Beintema JJ, and Dijkstra BW. (1994). Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure. 1994;2(12):1181-9. DOI:10.1016/s0969-2126(94)00120-0 |
- Terwisscha van Scheltinga AC, Armand S, Kalk KH, Isogai A, Henrissat B, and Dijkstra BW. (1995). Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry. 1995;34(48):15619-23. DOI:10.1021/bi00048a003 |