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!
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.
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]
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.
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]
Coming soon!
How transferases work, examples:
Coming Soon!
Coming Soon!
looks like this section will be on CoA Transferase in E.coli
Diseases include:
Coming Soon!
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:
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)
Here is a possible table I have been working on for the EC section. It just needs to be filled in:
-- WillPugarth ( talk) 07:35, 18 November 2013 (UTC)
Previous format:
Transferases are classified into these subclasses:
Images and formula for Galactose-1-phosphate uridyltransferase
EC 2.1 includes enzymes that transfer single-carbon groups. This category consists of methyl-, hydroxymethyl-, formyl-, carboxy-, carbamoyl-, and amidotransferases. <ref/ EC 2.1.3 http://www.chem.qmul.ac.uk/iubmb/enzyme/EC2/1/3/> Carbamoyltransferases, as an example, transfer a carbamoyl group from one molecule to another. <ref/ http://medical-dictionary.thefreedictionary.com/carbamoyltransferase> Carbamoyl groups follow the formula NH2CO <ref/ http://www.thefreedictionary.com/carbamoyl>. In ATCase such a transfer is written as Carbamyl phosphate + L-aspertate L-carbamyl aspartate + phosphate <ref/ http://actachemscand.dk/pdf/acta_vol_10_p0548-0566.pdf >, or graphically:
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 erythrose 4-phosphate + fructose 6-phosphate </ref http://enzyme.expasy.org/EC/2.2.1.2 >
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. [6] As an aminoacyltransferase, it catalyzes the following reaction: peptidyl-tRNAA + aminoacyl-tRNAB tRNAA + peptidyl aminoacyl-tRNAB. [7]
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. [8] 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. [9] This occurs via the following pathway: UDP-α-D-glucose + D-glucose UDP + lactose. [10]
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. [11] 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 L-cysteine + acetate. [12]
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). [13] 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. [14]
The reaction, for example, follows the following reaction: L-aspartate +2-oxoglutarate oxaloacetate + L-glutamate. [15]
While EC 2.7 includes enzymes that transfer phosphorus-containing groups, it also includes nuclotidyl transferases as well. [16] 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. [17] Once combined, the CDK-cyclin complex is capable of enacting its function within the cell cycle. [18]
The reaction catalyzed by CDK is as follows: ATP + a target protein ADP + a phosphoprotein. [19]
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. [21] A specific group of sulfotransferases are those that use PAPS as a sulfate group donor. [22] Within this group is alcohol sulfotransferase which has a broad targeting capacity. [23] Due to this, alcohol sulfotransferase is also known by several other names including "hydroxysteroid sulfotransferase," "steroid sulfokinase," and "estrogen sulfotransferase." [24] Decreases in its activity has been linked to human liver disease. [25] This transferase acts via the following reaction: 3'-phosphoadenylyl sulfate + an alcohol adenosine 3',5'bisphosphate + an alkyl sulfate. [26]
EC 2.9 includes enzymes that transfer selenium-containing groups. [27] 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). [28]
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. [29] This enzyme is a component of MoCo biosynthesis in Escherichia coli. [30] The reaction it catalyzes is as follows:
-- WillPugarth ( talk) 00:49, 25 November 2013 (UTC)
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. [31] This observance was later verified by the discovery of its reaction mechanism by Braunstein and Kritzmann in 1937. [32] Their analysis showed that this reversible reaction could be applied to other tissues. [33] This assertion was validated by Schoenheimer's work with radioisotopes as tracers in 1937. [34] [35] 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. [36]
transaminase uses puridoxal phosphate (B6) as a cofactor
Relation of structures between hydrolases and transferases
links at:
Classification of transferases continues to this day, with new ones being discovered frequently. [37] [38] An example of this is Pipe, a sulfotransferase involved in the dorsal-ventral patterning of Drosophilia. [39] Initially, the exact mechanism of Pipe was unknown, due to a lack of information on its substrate. [40] Research into Pipe's catalytic activity eliminated the likelihood of it being a heparan sulfate glycosaminoglycan. [41] Further research has shown that Pipe targets the ovarian structures for sulfation. [42] Pipe is currently classified as a Drosophilia heparan sulfate 2-O-sulfotransferase. [43]
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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!
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.
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]
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.
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]
Coming soon!
How transferases work, examples:
Coming Soon!
Coming Soon!
looks like this section will be on CoA Transferase in E.coli
Diseases include:
Coming Soon!
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:
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)
Here is a possible table I have been working on for the EC section. It just needs to be filled in:
-- WillPugarth ( talk) 07:35, 18 November 2013 (UTC)
Previous format:
Transferases are classified into these subclasses:
Images and formula for Galactose-1-phosphate uridyltransferase
EC 2.1 includes enzymes that transfer single-carbon groups. This category consists of methyl-, hydroxymethyl-, formyl-, carboxy-, carbamoyl-, and amidotransferases. <ref/ EC 2.1.3 http://www.chem.qmul.ac.uk/iubmb/enzyme/EC2/1/3/> Carbamoyltransferases, as an example, transfer a carbamoyl group from one molecule to another. <ref/ http://medical-dictionary.thefreedictionary.com/carbamoyltransferase> Carbamoyl groups follow the formula NH2CO <ref/ http://www.thefreedictionary.com/carbamoyl>. In ATCase such a transfer is written as Carbamyl phosphate + L-aspertate L-carbamyl aspartate + phosphate <ref/ http://actachemscand.dk/pdf/acta_vol_10_p0548-0566.pdf >, or graphically:
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 erythrose 4-phosphate + fructose 6-phosphate </ref http://enzyme.expasy.org/EC/2.2.1.2 >
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. [6] As an aminoacyltransferase, it catalyzes the following reaction: peptidyl-tRNAA + aminoacyl-tRNAB tRNAA + peptidyl aminoacyl-tRNAB. [7]
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. [8] 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. [9] This occurs via the following pathway: UDP-α-D-glucose + D-glucose UDP + lactose. [10]
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. [11] 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 L-cysteine + acetate. [12]
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). [13] 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. [14]
The reaction, for example, follows the following reaction: L-aspartate +2-oxoglutarate oxaloacetate + L-glutamate. [15]
While EC 2.7 includes enzymes that transfer phosphorus-containing groups, it also includes nuclotidyl transferases as well. [16] 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. [17] Once combined, the CDK-cyclin complex is capable of enacting its function within the cell cycle. [18]
The reaction catalyzed by CDK is as follows: ATP + a target protein ADP + a phosphoprotein. [19]
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. [21] A specific group of sulfotransferases are those that use PAPS as a sulfate group donor. [22] Within this group is alcohol sulfotransferase which has a broad targeting capacity. [23] Due to this, alcohol sulfotransferase is also known by several other names including "hydroxysteroid sulfotransferase," "steroid sulfokinase," and "estrogen sulfotransferase." [24] Decreases in its activity has been linked to human liver disease. [25] This transferase acts via the following reaction: 3'-phosphoadenylyl sulfate + an alcohol adenosine 3',5'bisphosphate + an alkyl sulfate. [26]
EC 2.9 includes enzymes that transfer selenium-containing groups. [27] 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). [28]
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. [29] This enzyme is a component of MoCo biosynthesis in Escherichia coli. [30] The reaction it catalyzes is as follows:
-- WillPugarth ( talk) 00:49, 25 November 2013 (UTC)
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. [31] This observance was later verified by the discovery of its reaction mechanism by Braunstein and Kritzmann in 1937. [32] Their analysis showed that this reversible reaction could be applied to other tissues. [33] This assertion was validated by Schoenheimer's work with radioisotopes as tracers in 1937. [34] [35] 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. [36]
transaminase uses puridoxal phosphate (B6) as a cofactor
Relation of structures between hydrolases and transferases
links at:
Classification of transferases continues to this day, with new ones being discovered frequently. [37] [38] An example of this is Pipe, a sulfotransferase involved in the dorsal-ventral patterning of Drosophilia. [39] Initially, the exact mechanism of Pipe was unknown, due to a lack of information on its substrate. [40] Research into Pipe's catalytic activity eliminated the likelihood of it being a heparan sulfate glycosaminoglycan. [41] Further research has shown that Pipe targets the ovarian structures for sulfation. [42] Pipe is currently classified as a Drosophilia heparan sulfate 2-O-sulfotransferase. [43]
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