User:WillPugarth/sandbox

From Wikipedia, the free encyclopedia

Introduction

This is my sandbox page. I am just learning how to edit my sandbox so that I can practice creating content and editing it. I am following along with the Training modules in Wikipedia. Hopefully it will be fairly straightforward!

Summary of the Five Pillars

Here is my explanation of the Five Pillars ^[1] of Wikipedia, the Free Encyclopedia.

The Blue pillar refers to the inherent nature of Wikipedia as an encyclopedia and not a directory or an ad agency.

The Green pillar references the goal of Wikipedia to be neutral in perspective.

The Yellow pillar demonstrates the site's goal of having free content available to everyone.

The Orange pillar requires users to follow etiquette established by Wikipedia users.

The Red pillar defines the rule structure of Wikipedia as being "spirit" based and not extremely restrictive.

More Practice

Here's a bold text option: Bold

And here's a link to something: Pug and Hogarth

Italics are used for genes

Headlines are used on Wikipedia.^[2]

Summary of characteristics of target article

Wikipedia article quality is determined in several grades. The highest levels of quality are FA, GA, and A, However for our assignment, we will be attempting to take a "stub" class article and bring it up to B (or higher) level ^[3]

In order for an article to be considered a "B" level article, it must have enough information to be relatively useful and be arrange so that the information is accessible. Further, ideally it would have sources cited and some amount of images/diagrams.

Improvements that could be made to such an article include improving style, upgrading graphics and illustrations, as well as adding content and more reputable and effective sources.

Assessing PubMed articles

The advancement of biofuel systems

Recently, the idea that various organisms can be used to power or even produce necessary components has become a popular avenue in advancing biofuel systems. It is known that species of both bacteria and algae are capable of utilizing carbon fixation.^[4] Cyanobacteria, which can be made capable of producing FFAs for fuel industry purposes, possess genes that make them particularly resistant to FFA production cellular damage.^[5] In addition to cyanobacteria, algae have also been explored as a possible means to alternative fuel cells. In particular, green algae has been explored as a possible replacement for platinum in battery electrodes.^[4]

Unit 7 References and Outline

References for consideration

Introductory citations

http://ghr.nlm.nih.gov/glossary=transferase

http://www.britannica.com/EBchecked/topic/602553/transferase

http://www.uniprot.org/keywords/KW-0808

pfam.sanger.ac.uk/family/PF02458

http://www.ncbi.nlm.nih.gov/pubmed/8443790 (aldehyde transferases)

http://ghr.nlm.nih.gov/condition/succinyl-coa3-ketoacid-coa-transferase-deficiency (Ketone transferase)

http://www.reference.md/files/D019/mD019880.html (aldehyde-ketone transferases)

http://www.yeastgenome.org/cgi-bin/GO/goTerm.pl?goid=16765 (aryl or alkyl transferase, non methyl)

https://en.wikipedia.org/wiki/Elevated_transaminases (transaminases)

http://www.ncbi.nlm.nih.gov/pubmed/17158705 (phospotransferase)

http://toxsci.oxfordjournals.org/content/90/1/5.full (sulfotransferase)

http://www.brenda-enzymes.org/php/result_flat.php4?ecno=2.9.1.1 (selenium transferases)

Types of transferases

methyltransferase: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3705300/

acyltransferase: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3762864/ (this one actually has a lot of information on several types of transferases)

glycosyl transferase: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3390697/

Structural Citations

Coming soon!

Biological Functions

How transferases work, examples:

Terminal transferases: http://www.vivo.colostate.edu/hbooks/genetics/biotech/enzymes/tt.html

find various other types of transferases and amalgamate them into descriptions: ie, "Some transferases . . ., while others . . . "

Some examples of important transferases and how they work, on a less specific level than the main articles for those compounds

Regulation Citations

Cofactor Citations

Coming Soon!

Inhibition Citations

Coming Soon!

Kinetics Citations

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC232864/ --> article on kinematics of CoA Transferase

http://www.sciencedirect.com/science/article/pii/000398617590003X --> another on the same enzyme

looks like this section will be on CoA Transferase in E.coli

Disease Citations

Diseases include:

CPT deficiency: http://mda.org/disease/metabolic-diseases-of-muscle/CPT-deficiency

smoking-related coronary artery disease: http://www.ncbi.nlm.nih.gov/pubmed/10729397 and http://www.ncbi.nlm.nih.gov/pubmed/15088107

In mouse Alzheimer's disease: http://www.jbc.org/content/early/2013/10/17/jbc.M113.503904.abstract

Biotech/Medicine Citations

Coming Soon!

Possible Outline

1) the history and background for transferases;

2) kinds of transferases

3) the general structure of transferases;

4) how transferases work;

5) the energy considerations of transferases;

6) any cofactors, coenzymes, etc.;

7) How are transferases controlled/regulated;

8) Any diseases transferase is involved in;

9) Biotech/industrial/medical research uses relating to transferase

Possible Images

Need to find or make an image including the transferase equation currently given in the text Also need to add images relating to any examples given

--WillPugarth (talk) 19:45, 21 October 2013 (UTC) I'm not sure what you want,but here are some images we can use:

http://upload.wikimedia.org/wikipedia/commons/c/ce/Galactose-1-phosphate_uridylyltransferase_1GUP.png

http://upload.wikimedia.org/wikipedia/commons/c/cc/1400x1048_pdh_regulation.png

http://upload.wikimedia.org/wikipedia/commons/6/6d/Phe_Tyr.png

http://upload.wikimedia.org/wikipedia/commons/0/0b/Tryptophan_metabolism.png

Do you think you would want an image for each type? Do you want specific reactions or just images of the transferases themselves? Adimart1 (talk) 02:32, 28 October 2013 (UTC)

These are fantastic! We probably want one molecule example for the header image, and the rest can be reactions. But what you added here should be more than enough. Then we can just write up sections that explain the reactions when it is time to revise the sections related to the images you found. These will save us a lot of time and help us to bulk up the article. --WillPugarth (talk) 04:11, 29 October 2013 (UTC)

Glad you like them. I'm not much of a writer, but I am a really good researcher. Adimart1 (talk) 04:35, 29 October 2013 (UTC)

EC Table

Here is a possible table I have been working on for the EC section. It just needs to be filled in:

More information EC number, Examples ...

Classification of transferases into subclasses:
EC number	Examples	Description
EC 2.1	methyltransferase, formyltransferase, carboxytransferase, and amidotransferase	Transfers single-carbon groups
EC 2.2	transketolase and transaldolase	Transfers aldehyde or ketone groups
EC 2.3	acyltransferase	Transfers acyl groups or groups that become alkyl groups during transfer
EC 2.4	glycosyltransferase, hexosyltransferase, and pentosyltransferase	Transfers glycosyl groups, as well as hexoses and pentoses
EC 2.5	riboflavin synthase and chlorophyll synthase	Transfers alkyl or aryl groups, other than methyl groups
EC 2.6	transaminase, amidotransferase, and oximinotransferase	Transfers nitrogenous groups
EC 2.7	phosphotransferase, polymerase, and kinase	Transfers phosphorous-containing groups; subclasses are based on the acceptor (e.g. alcohol, carboxyl, etc.)
EC 2.8	sulfurtransferase and sulfotransferase	Transfers sulfur-containing groups
EC 2.9	selenotransferase	Transfers selenium-containing groups
EC 2.10	molybdenumtransferase and tungstentransferase	Transfers molybdenum or tungsten

--WillPugarth (talk) 07:35, 18 November 2013 (UTC)

Previous format:

Transferases are classified into these subclasses:

EC 2.1 includes enzymes that transfer single-carbon groups (e.g. methyltransferases, formyltransferases, carboxytransferases, and amidotransferases)
EC 2.2 includes enzymes that transfer aldehyde or ketone groups
EC 2.3 includes enzymes that transfer acyl groups (acyltransferases) or acyl groups that become alkyl groups during the transfer
EC 2.4 includes enzymes that transfer glycosyl groups glycosyltransferases, as well as hexosyltransferases and pentosyltransferases
EC 2.5 includes enzymes that transfer alkyl or aryl groups, other than methyl groups
EC 2.6 includes enzymes that transfer nitrogenous groups (e.g. transaminase, amidinotransferases, and oximinotransferases)
EC 2.7 includes enzymes that transfer phosphorus-containing groups (e.g.phosphotransferase), and is further subdivided based on what type of group acts as the acceptor (e.g. alcohol, carboxyl, etc.) and activity (e.g. polymerase and kinase)
EC 2.8 includes enzymes that transfer sulfur-containing groups (e.g. sulfurtransferase and sulfotransferase)
EC 2.9 includes enzymes that transfer selenium-containing groups (selenotransferases)
EC 2.10 includes enzymes that transfer molybdenum or tungsten-containing groups (e.g. molybdenumtransferases and tungstentransferases)

New images

Images and formula for Galactose-1-phosphate uridyltransferase

Additions to Transferase Classifications section

EC 2.1: single carbon transferases

EC 2.1 includes enzymes that transfer single-carbon groups. This category consists of methyl-, hydroxymethyl-, formyl-, carboxy-, carbamoyl-, and amidotransferases. ^[6] Carbamoyltransferases, as an example, transfer a carbamoyl group from one molecule to another. ^[7] As an aminoacyltransferase, it catalyzes the following reaction: peptidyl-tRNA_A + aminoacyl-tRNA_B $\rightleftharpoons$ tRNA_A + peptidyl aminoacyl-tRNA_B.^[8]

EC 2.4: glycosyl, hexosyl, and pentosyl transferases

EC 2.4 includes enzymes that transfer glycosyl groups, as well as those that transfer hexose and pentose. Glycosyltransferase is a subcategory of transferase that is involved in biosynthesis of disaccharides and polysaccharides through transfer of monosaccharides to other molecules.^[9] An example of a prominent glycosyltransferase is lactose synthase which is a dimer possessing two protein subunits. Its primary action is to produce lactose from glucose and UDP-glucose.^[10] This occurs via the following pathway: UDP-α-D-glucose + D-glucose $\rightleftharpoons$ UDP + lactose.^[11]

EC 2.5: alkyl and aryl transferases

EC 2.5 includes enzymes that transfer alkyl or aryl groups, but does not include methyl groups. This is in contrast to functional groups that become alkyl groups when transferred, as those are included in EC 2.3. EC 2.5 currently only possesses one sub-class: Alkyl and aryl transferases.^[12] Cysteine synthase, for example, catalyzes the formation of acetic acids and cysteine from O₃-acetyl-L-serine and hydrogen sulfide: O₃-acetyl-L-serine + H₂S $\rightleftharpoons$ L-cysteine + acetate.^[13]

EC 2.6: nitrogenous transferases

The grouping consistent with transfer of nitrogenous groups is EC 2.6. This includes enzymes like transaminase (also known as "aminotransferase"), and a very small number of oximinotransferases and other nitrogen group transferring enzymes. EC 2.6 previously included amidinotransferase but it has since been reclassified as a subcategory of EC 2.1 (single-carbon transferring enzymes).^[14] In the case of aspartate transaminase, which can act on tyrosine, phenylalanine, and tryptophan, it reversibly transfers an amino group from one molecule to the other.^[15]

The reaction, for example, follows the following reaction: L-aspartate +2-oxoglutarate $\rightleftharpoons$ oxaloacetate + L-glutamate.^[16]

EC 2.7: phosphorus transferases

While EC 2.7 includes enzymes that transfer phosphorus-containing groups, it also includes nuclotidyl transferases as well.^[17] Sub-category phosphotransferase is divided up in categories based on the type of group that accepts the transfer.(CITE EC2 Intro) Groups that are classified as phosphate acceptors include: alcohols, carboxy groups, nitrogenous groups, and phosphate groups. (CITE EC2 list) Further constituents of this subclass of transferases are various kinases. A prominent kinase is cyclin-dependent kinase (or CDK), which comprises a sub-family of protein kinases. As their name implies, CDKs are heavily dependent on specific cyclin molecules for activation.^[18] Once combined, the CDK-cyclin complex is capable of enacting its function within the cell cycle.^[19]

The reaction catalyzed by CDK is as follows: ATP + a target protein $\rightarrow$ ADP + a phosphoprotein.^[20]

EC 2.8: sulfur transferases

Transfer of sulfur-containing groups is covered by EC 2.8 and is subdivided into the subcategories of sulfurtransferases, sulfotransferases, and CoA-transferases, as well as enzymes that transfer alkylthio groups.^[22] A specific group of sulfotransferases are those that use PAPS as a sulfate group donor.^[23] Within this group is alcohol sulfotransferase which has a broad targeting capacity.^[24] Due to this, alcohol sulfotransferase is also known by several other names including "hydroxysteroid sulfotransferase," "steroid sulfokinase," and "estrogen sulfotransferase."^[25] Decreases in its activity has been linked to human liver disease.^[26] This transferase acts via the following reaction: 3'-phosphoadenylyl sulfate + an alcohol $\rightleftharpoons$ adenosine 3',5'bisphosphate + an alkyl sulfate.^[27]

EC 2.9: selenium transferases

EC 2.9 includes enzymes that transfer selenium-containing groups.^[28] This category only contains two transferases, and thus is one of the smallest categories of transferase. Selenocysteine synthase, whcih was first added to the classification system in 1999, converts seryl-tRNA(Sec UCA) into selenocysteyl-tRNA(Sec UCA).^[29]

EC 2.10: metal transferases

The category of EC 2.10 includes enzymes that transfer molybdenum or tungsten-containing groups. However as of 2011, only one enzyme has been added: molybdopterin molybdotransferase.^[30] This enzyme is a component of MoCo biosynthesis in Escherichia coli.^[31] The reaction it catalyzes is as follows:

--WillPugarth (talk) 00:49, 25 November 2013 (UTC)

Other Additions

History additions

1930s Transamination, or the transfer of an amine (or NH₂) group from an amino acid to a keto acid by an aminotransferase (also known as a "transaminase"), was first noted in 1930 by D. M. Needham, after observing the disappearance of glutamic acid added to pigeon breast muscle.^[32] This observance was later verified by the discovery of its reaction mechanism by Braunstein and Kritzmann in 1937.^[33] Their analysis showed that this reversible reaction could be applied to other tissues.^[34] This assertion was validated by Schoenheimer's work with radioisotopes as tracers in 1937.^[35]^[36] This in turn would pave the way for the possibility that similar transfers were a primary means of producing most amino acids via amino transfer.^[37]

Cofactors

transaminase uses puridoxal phosphate (B6) as a cofactor

Mechanisms

Relation of structures between hydrolases and transferases

links at:

https://en.wikibooks.org/wiki/Structural_Biochemistry/Specific_Enzymes_and_Catalytic_Mechanisms/Enzyme_Classification

http://www.sciencedirect.com/science/article/pii/S0144861700002496

Recent developments

Classification of transferases continues to this day, with new ones being discovered frequently.^[38]^[39] An example of this is Pipe, a sulfotransferase involved in the dorsal-ventral patterning of Drosophilia.^[40] Initially, the exact mechanism of Pipe was unknown, due to a lack of information on its substrate.^[41] Research into Pipe's catalytic activity eliminated the likelihood of it being a heparan sulfate glycosaminoglycan.^[42] Further research has shown that Pipe targets the ovarian structures for sulfation.^[43] Pipe is currently classified as a Drosophilia heparan sulfate 2-O-sulfotransferase.^[44]

Notes

[1]
Five pillars Wikipedia, The Free Encyclopedia. Retrieved September 12, 2013.
[2]
Headline Wikipedia, The Free Encyclopedia. Retrieved September 12, 2013.
[3]
Johns Hopkins University Molecular Biology Wiki Assignment. Wikipedia, The Free Encyclopedia. Retrieved September 30, 2013.
[4]
Chen, W. J.; Lee, M. H.; Thomas, J. L.; Lu, P. H.; Li, M. H.; Lin, H. Y. (2013 Oct 6). "The Microcontact Imprinting of Algae on Poly(ethylene-co-vinyl alcohol) for Biofuel Cells". ACS Applied Materials & Interfaces. 5 (21): 11123–11128. doi:10.1021/am403313p. PMID 24095224. {{cite journal}}: Check date values in: |date= (help)
[5]
Ruffing, AM (2013 Aug 6). "RNA-Seq analysis and targeted mutagenesis for improved free fatty acid production in an engineered cyanobacterium". Biotechnology for Biofuels. 6 (1): 113. doi:10.1186/1754-6834-6-113. PMC 3750487. PMID 23919451. {{cite journal}}: Check date values in: |date= (help)CS1 maint: unflagged free DOI (link)
[6]
[7]
Carbamoyl groups follow the formula NH2CO <ref/ http://www.thefreedictionary.com/carbamoyl>. In ATCase such a transfer is written as Carbamyl phosphate + L-aspertate $\rightarrow$ L-carbamyl aspartate + phosphate <ref/ http://actachemscand.dk/pdf/acta_vol_10_p0548-0566.pdf >, or graphically:
EC 2.2: aldehyde and ketone transferases
EC 2.2 includes enzymes that transfer aldehyde or ketone groups. This category consists of various transketolases and transaldolases. </ref http://www.chem.qmul.ac.uk/iubmb/enzyme/EC2/2/1/ > transaldolase, the namesake of aldehyde transferases, is an important part of the pentose phosphate pathway. </ref http://www.rpi.edu/dept/bcbp/molbiochem/MBWeb/mb2/part1/pentose.htm > The reaction it catalyzes consists of a transfer of a dihydroxyacetone functional group to G3P. The reaction is as follows: sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate $\rightleftharpoons$ erythrose 4-phosphate + fructose 6-phosphate </ref http://enzyme.expasy.org/EC/2.2.1.2 >
EC 2.3: acyl transferases
EC 2.3 includes enzymes that transfer acyl groups or acyl groups that become alkyl groups during the process of being transferred. Further, this category also differentiates between amino-acyl and non-amino-acyl groups. Peptidyl transferase is a ribozyme that facilitates formation of peptide bonds during translation.<ref>Voorhees, R. M.; Weixlbaumer, A.; Loakes, D.; Kelley, A. C.; Ramakrishnan, V. (2009 May). "Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome". Nature Structural & Molecular Biology. 16 (5): 528–33. doi:10.1038/nsmb.1577. PMC 2679717. PMID 19363482. {{cite journal}}: Check date values in: |date= (help)
[8]
"ENZYME entry: EC 2.3.2.12". ExPASy: Bioinformatics Resource Portal. Swiss Institute of Bioinformatics. Retrieved 26 November 2013.
[9]
"Keyword Glycosyltransferase". UniProt. UniProt Consortium. Retrieved 26 November 2013.
[10]
Fitzgerald, D.K. (1970). "α-Lactalbumin and the Lactose Synthetase Reaction". Journal of Biological Chemistry. 245 (8): 2103–2108. doi:10.1016/S0021-9258(18)63212-0. PMID 5440844. Retrieved 26 November 2013. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
[11]
"ENZYME entry: EC 2.4.1.22". ExPASy: Bioinformatics Resource Portal. Swiss Institute of Bioinformatics. Retrieved 26 November 2013.
[12]
"EC 2.5". IntEnz. European Molecular Biology Laboratory. Retrieved 26 November 2013.
[13]
Qabazard, B.; Ahmed, S.; Li, L.; Arlt, V. M.; Moore, P. K.; Stürzenbaum, S. R. (2013 Nov 8). "C. elegans Aging Is Modulated by Hydrogen Sulfide and the sulfhydrylase/cysteine Synthase cysl-2". PLOS ONE. 8 (11): e80135. doi:10.1371/journal.pone.0080135. PMC 3832670. PMID 24260346. {{cite journal}}: Check date values in: |date= (help)CS1 maint: article number as page number (link)
[14]
"EC 2.6.2". IUBMB Enzyme Nomenclatur. Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Retrieved 28 November 2013.
[15]
Kirsch, JF (1984 Apr 15). "Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure". Journal of Molecular Biology. 174 (3): 497–525. doi:10.1016/0022-2836(84)90333-4. PMID 6143829. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
[16]
"ENZYME entry:2.6.1.1". ExPASy: Bioinformatics Resource Portal. Swiss Institute of Bioinformatics. Retrieved 28 November 2013.
[17]
"EC 2.7". School of Biological & Chemical Sciences at Queen Mary, University of London. Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Retrieved 4 December 2013.
[18]
Yee, A.; Wu, L.; Liu, L.; Kobayashi, R.; Xiong, Y.; Hall, F. L. (1996 Jan 5). "Biochemical characterization of the human cyclin-dependent protein kinase activating kinase. Identification of p35 as a novel regulatory subunit". The Journal of Biological Chemistry. 271 (1): 471–7. doi:10.1074/jbc.271.1.471. PMID 8550604. {{cite journal}}: Check date values in: |date= (help)
[19]
Lewis, Ricki (2008). Human genetics : concepts and applications (8th ed.). Boston: McGraw-Hill/Higher Education. p. 32. ISBN 978-0-07-299539-8.
[20]
"ENZYME Entry: EC 2.7.11.22". ExPASy: Bioinformatics Resource Portal. Swiss Institute of Bioinformatics. Retrieved 4 December 2013.
[21]
"1aqy Summary". Protein Data Bank in Europe Bringing Structure to Biology. The European Bioinformatics Institute. Retrieved 11 December 2013.
[22]
"EC 2.8 Transferring Sulfur-Containing Groups". School of Biological & Chemical Sciences at Queen Mary, University of London. Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Retrieved 11 December 2013.
[23]
Negishi, M.; Pedersen, L. G.; Petrotchenko, E.; Shevtsov, S.; Gorokhov, A.; Kakuta, Y.; Pedersen, L. C. (2001 Jun 15). "Structure and function of sulfotransferases". Archives of Biochemistry and Biophysics. 390 (2): 149–57. doi:10.1006/abbi.2001.2368. PMID 11396917. {{cite journal}}: Check date values in: |date= (help)
[24]
"EC 2.8 Transferring Sulfur-Containing Groups". School of Biological & Chemical Sciences at Queen Mary, University of London. Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Retrieved 11 December 2013.
[25]
"Enzyme 2.8.2.2". Kegg: DBGET. Kyoto University Bioinformatics Center. Retrieved 11 December 2013.
[26]
Ou, Z (2013 Jan). "Regulation of the human hydroxysteroid sulfotransferase (SULT2A1) by RORα and RORγ and its potential relevance to human liver diseases". Molecular Endocrinology (Baltimore, Md.). 27 (1): 106–15. doi:10.1210/me.2012-1145. PMC 3545217. PMID 23211525. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
[27]
Sekura, RD (1979 May). "Assay of sulfotransferases". Analytical Biochemistry. 95 (1): 82–6. doi:10.1016/0003-2697(79)90188-x. PMID 495970. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
[28]
"EC 2.9.1". School of Biological & Chemical Sciences at Queen Mary, University of London. Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Retrieved 11 December 2013.
[29]
Forchhammer, K (1991 Apr 5). "Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence". The Journal of Biological Chemistry. 266 (10): 6324–8. doi:10.1016/S0021-9258(18)38121-3. PMID 2007585. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
[30]
"EC 2.10.1". School of Biological & Chemical Sciences at Queen Mary, University of London. Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Retrieved 11 December 2013.
[31]
Nichols, J. D.; Xiang, S.; Schindelin, H.; Rajagopalan, K. V. (2007 Jan 9). "Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft". Biochemistry. 46 (1): 78–86. doi:10.1021/bi061551q. PMC 1868504. PMID 17198377. {{cite journal}}: Check date values in: |date= (help)
[32]
Cohen, PP (1939 Sep). "Transamination in pigeon breast muscle". The Biochemical Journal. 33 (9): 1478–87. doi:10.1042/bj0331478. PMC 1264599. PMID 16747057. {{cite journal}}: Check date values in: |date= (help)
[33]
Snell, Esmond E.; Jenkins, W. Terry (1959). "The mechanism of the transamination reaction". Journal of Cellular and Comparative Physiology. 54 (S1): 161–177. doi:10.1002/jcp.1030540413. PMID 13832270. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: date and year (link)
[34]
Braunstein, A. E.; Kritzmann, M. G. (18 September 1937). "Formation and Breakdown of Amino-acids by Inter-molecular Transfer of the Amino Group". Nature. 140 (3542): 503–504. doi:10.1038/140503b0. S2CID 4009655.
[35]
Schoenheimer, Rudolf (1949). The Dynamic State of Body Constituents. Hafner Publishing Co Ltd. ISBN 0028518004. {{cite book}}: ISBN / Date incompatibility (help)
[36]
Guggenheim, KY (1991 Nov). "Rudolf Schoenheimer and the concept of the dynamic state of body constituents". The Journal of Nutrition. 121 (11): 1701–4. doi:10.1093/jn/121.11.1701. PMID 1941176. {{cite journal}}: Check date values in: |date= (help)
[37]
Hird, F. J. R.; Rowsell, E. V. (23 September 1950). "Additional Transaminations by Insoluble Particle Preparations of Rat Liver". Nature. 166 (4221): 517–518. doi:10.1038/166517a0. PMID 14780123. S2CID 4215187.
[38]
Lambalot, R. H.; Gehring, A. M.; Flugel, R. S.; Zuber, P.; Lacelle, M.; Marahiel, M. A.; Reid, R.; Khosla, C.; Walsh, C. T. (1996 Nov). "A new enzyme superfamily - the phosphopantetheinyl transferases". Chemistry & Biology. 3 (11): 923–36. doi:10.1016/s1074-5521(96)90181-7. PMID 8939709. {{cite journal}}: Check date values in: |date= (help)
[39]
Wongtrakul, J (2010 Mar). "Expression and characterization of three new glutathione transferases, an epsilon (AcGSTE2-2), omega (AcGSTO1-1), and theta (AcGSTT1-1) from Anopheles cracens (Diptera: Culicidae), a major Thai malaria vector". Journal of Medical Entomology. 47 (2): 162–71. doi:10.1603/me09132. PMID 20380296. S2CID 23558834. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
[40]
Sen, J.; Goltz, J. S.; Stevens, L.; Stein, D. (1998 Nov 13). "Spatially restricted expression of pipe in the Drosophila egg chamber defines embryonic dorsal-ventral polarity". Cell. 95 (4): 471–81. doi:10.1016/s0092-8674(00)81615-3. PMID 9827800. S2CID 27722532. {{cite journal}}: Check date values in: |date= (help)
[41]
Moussian, B.; Roth, S. (2005 Nov 8). "Dorsoventral axis formation in the Drosophila embryo--shaping and transducing a morphogen gradient". Current Biology : CB. 15 (21): R887-99. doi:10.1016/j.cub.2005.10.026. PMID 16271864. S2CID 15984116. {{cite journal}}: Check date values in: |date= (help)
[42]
Zhu, X.; Sen, J.; Stevens, L.; Goltz, J. S.; Stein, D. (2005 Sep). "Drosophila pipe protein activity in the ovary and the embryonic salivary gland does not require heparan sulfate glycosaminoglycans". Development (Cambridge, England). 132 (17): 3813–22. doi:10.1242/dev.01962. PMID 16049108. S2CID 16046484. {{cite journal}}: Check date values in: |date= (help)
[43]
Zhang, Z (2009 Jul 28). "Sulfation of eggshell components by Pipe defines dorsal-ventral polarity in the Drosophila embryo". Current Biology : CB. 19 (14): 1200–5. doi:10.1016/j.cub.2009.05.050. PMC 2733793. PMID 19540119. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
[44]
Xu, D.; Song, D.; Pedersen, L. C.; Liu, J. (2007 Mar 16). "Mutational study of heparan sulfate 2-O-sulfotransferase and chondroitin sulfate 2-O-sulfotransferase". The Journal of Biological Chemistry. 282 (11): 8356–67. doi:10.1074/jbc.M608062200. PMID 17227754. {{cite journal}}: Check date values in: |date= (help)

More Practice

The advancement of biofuel systems

References for consideration

Introductory citations

Types of transferases

Structural Citations

Biological Functions

Regulation Citations

Cofactor Citations

Inhibition Citations

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Additions to Transferase Classifications section

EC 2.1: single carbon transferases

EC 2.4: glycosyl, hexosyl, and pentosyl transferases

EC 2.5: alkyl and aryl transferases

EC 2.6: nitrogenous transferases

EC 2.7: phosphorus transferases

EC 2.8: sulfur transferases

EC 2.9: selenium transferases

EC 2.10: metal transferases

History additions

Cofactors

Mechanisms

Recent developments

EC 2.2: aldehyde and ketone transferases

EC 2.3: acyl transferases

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