User:Sydney Park - Revision history

Eran Hodis at 06:32, 18 November 2009

Eran Hodis — Wed, 18 Nov 2009 06:32:49 GMT

←Older revision		Revision as of 06:32, 18 November 2009
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		+	I am a undergradute student at Capital University majoring in Biology/Pre-vet.
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	'''Name of enzyme''': Enolase or phosphopyruvate dehydratase		'''Name of enzyme''': Enolase or phosphopyruvate dehydratase

Sydney Park at 21:16, 17 November 2009

Sydney Park — Tue, 17 Nov 2009 21:16:02 GMT

←Older revision		Revision as of 21:16, 17 November 2009
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	<scene name='User:Sydney_Park/Blah/1'>TextToBeDisplayed</scene>		<scene name='User:Sydney_Park/Blah/1'>TextToBeDisplayed</scene>
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		+	<applet load='3F48' size='300' frame='true' align='right' caption='Insert caption here' />

Sydney Park: BLah

Sydney Park — Tue, 17 Nov 2009 21:14:18 GMT

BLah

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	Citations: Wikipedia. <http://en.wikipedia.org/wiki/Fumarase>, Wikipedia. <http://en.wikipedia.org/wiki/Enolase>, University of Wisconsin- Eau Claire. <http://www.chem.uwec.edu/Webpapers_F99/Pages/Webpapers_F99/golnercm/Pages/descrip.html>, Virtual Chembook. Elmhurst College. <http://www.elmhurst.edu/~chm/vchembook/601glycolysisrx.html>		Citations: Wikipedia. <http://en.wikipedia.org/wiki/Fumarase>, Wikipedia. <http://en.wikipedia.org/wiki/Enolase>, University of Wisconsin- Eau Claire. <http://www.chem.uwec.edu/Webpapers_F99/Pages/Webpapers_F99/golnercm/Pages/descrip.html>, Virtual Chembook. Elmhurst College. <http://www.elmhurst.edu/~chm/vchembook/601glycolysisrx.html>
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		+	<scene name='User:Sydney_Park/Blah/1'>TextToBeDisplayed</scene>

Sydney Park at 21:09, 17 November 2009

Sydney Park — Tue, 17 Nov 2009 21:09:36 GMT

←Older revision		Revision as of 21:09, 17 November 2009
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-	<scene name='User:Sydney_Park/Leuthydro/1'>~~TextToBeDisplayed~~</scene>	+	<scene name='User:Sydney_Park/Leuthydro/1'>Hydrophilic</scene>

Sydney Park at 21:08, 17 November 2009

Sydney Park — Tue, 17 Nov 2009 21:08:18 GMT

←Older revision	Revision as of 21:08, 17 November 2009
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	+	<scene name='User:Sydney_Park/Leuthydro/1'>TextToBeDisplayed</scene>

Sydney Park at 01:17, 16 November 2009

Sydney Park — Mon, 16 Nov 2009 01:17:05 GMT

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	There are two classes of Fumarases, which depend on the arrangement of their relative subunit, their metal requirement, and their thermal stability. Class I Fumarases can change their state or become inactive when exposed to heat or radiation. They are sensitive to superoxide anions and Fe2+ dependent. Class II Fumarases are found in eukaryotes and prokaryotes. They are iron-independent and thermal-stable.		There are two classes of Fumarases, which depend on the arrangement of their relative subunit, their metal requirement, and their thermal stability. Class I Fumarases can change their state or become inactive when exposed to heat or radiation. They are sensitive to superoxide anions and Fe2+ dependent. Class II Fumarases are found in eukaryotes and prokaryotes. They are iron-independent and thermal-stable.
	Fumarase deficiency is an autosomal recessive metabolic disorder distinguished by a deficiency of the enzyme Fumarate hydratase and indicated by an excess of Fumaric acid in the urine. It is common of infants with neurologic abnormalities and its potential causes include cytosolic and mitochondrial forms of Fumarase.		Fumarase deficiency is an autosomal recessive metabolic disorder distinguished by a deficiency of the enzyme Fumarate hydratase and indicated by an excess of Fumaric acid in the urine. It is common of infants with neurologic abnormalities and its potential causes include cytosolic and mitochondrial forms of Fumarase.
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		+	'''Overview of Fumarase''':
		+	<scene name='User:Sydney_Park/Overview_of_fumarase/1'>Overview</scene>
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		+	'''Secondary Structure of Fumarase''':
		+	<scene name='User:Sydney_Park/Secondary_structure/1'>Secondary Structure</scene>

Sydney Park at 01:02, 16 November 2009

Sydney Park — Mon, 16 Nov 2009 01:02:30 GMT

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	Enolase is present in all tissues and organisms with the ability to do glycolysis or fermentation. Recent studies have Enolase concentration samples in order to determine certain conditions and their severity. For instance, high concentrations of Enolase in cerebrospinal fluid (CSF) are more strongly associated with astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase. High concentrations of Enolase in the CSF are also linked to the fastest rate of tumor growth and increased chances of heart attack or stroke.		Enolase is present in all tissues and organisms with the ability to do glycolysis or fermentation. Recent studies have Enolase concentration samples in order to determine certain conditions and their severity. For instance, high concentrations of Enolase in cerebrospinal fluid (CSF) are more strongly associated with astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase. High concentrations of Enolase in the CSF are also linked to the fastest rate of tumor growth and increased chances of heart attack or stroke.
	Enolase can be competitively inhibited by fluoride for the substrate 2-PGA. In drinking water with added fluorination, oral bacteria Enolase activity is inhibited without harmed humans. This works to prevent cavities.		Enolase can be competitively inhibited by fluoride for the substrate 2-PGA. In drinking water with added fluorination, oral bacteria Enolase activity is inhibited without harmed humans. This works to prevent cavities.
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		+	'''Overview of Enolase''':
		+	<scene name='User:Sydney_Park/Overview/1'>Overview</scene>

	'''Secondary Structure of Enolase''':		'''Secondary Structure of Enolase''':
-	<scene name='User:Sydney_Park/Secondary_structure_of_enolase/1'>~~Enolase~~</scene>	+	<scene name='User:Sydney_Park/Secondary_structure_of_enolase/1'>Secondary Structure</scene>

Sydney Park at 00:59, 16 November 2009

Sydney Park — Mon, 16 Nov 2009 00:59:13 GMT

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	'''Secondary Structure of Enolase''':		'''Secondary Structure of Enolase''':
-	<scene name='User:Sydney_Park/Secondary_structure_of_enolase/1'>~~TextToBeDisplayed~~</scene>	+	<scene name='User:Sydney_Park/Secondary_structure_of_enolase/1'>Enolase</scene>

Sydney Park at 00:57, 16 November 2009

Sydney Park — Mon, 16 Nov 2009 00:57:04 GMT

←Older revision		Revision as of 00:57, 16 November 2009
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	Enolase is present in all tissues and organisms with the ability to do glycolysis or fermentation. Recent studies have Enolase concentration samples in order to determine certain conditions and their severity. For instance, high concentrations of Enolase in cerebrospinal fluid (CSF) are more strongly associated with astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase. High concentrations of Enolase in the CSF are also linked to the fastest rate of tumor growth and increased chances of heart attack or stroke.		Enolase is present in all tissues and organisms with the ability to do glycolysis or fermentation. Recent studies have Enolase concentration samples in order to determine certain conditions and their severity. For instance, high concentrations of Enolase in cerebrospinal fluid (CSF) are more strongly associated with astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase. High concentrations of Enolase in the CSF are also linked to the fastest rate of tumor growth and increased chances of heart attack or stroke.
	Enolase can be competitively inhibited by fluoride for the substrate 2-PGA. In drinking water with added fluorination, oral bacteria Enolase activity is inhibited without harmed humans. This works to prevent cavities.		Enolase can be competitively inhibited by fluoride for the substrate 2-PGA. In drinking water with added fluorination, oral bacteria Enolase activity is inhibited without harmed humans. This works to prevent cavities.
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		+	'''Secondary Structure of Enolase''':
		+	<scene name='User:Sydney_Park/Secondary_structure_of_enolase/1'>TextToBeDisplayed</scene>

Sydney Park at 00:42, 16 November 2009

Sydney Park — Mon, 16 Nov 2009 00:42:49 GMT

←Older revision		Revision as of 00:42, 16 November 2009
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	There are two classes of Fumarases, which depend on the arrangement of their relative subunit, their metal requirement, and their thermal stability. Class I Fumarases can change their state or become inactive when exposed to heat or radiation. They are sensitive to superoxide anions and Fe2+ dependent. Class II Fumarases are found in eukaryotes and prokaryotes. They are iron-independent and thermal-stable.		There are two classes of Fumarases, which depend on the arrangement of their relative subunit, their metal requirement, and their thermal stability. Class I Fumarases can change their state or become inactive when exposed to heat or radiation. They are sensitive to superoxide anions and Fe2+ dependent. Class II Fumarases are found in eukaryotes and prokaryotes. They are iron-independent and thermal-stable.
	Fumarase deficiency is an autosomal recessive metabolic disorder distinguished by a deficiency of the enzyme Fumarate hydratase and indicated by an excess of Fumaric acid in the urine. It is common of infants with neurologic abnormalities and its potential causes include cytosolic and mitochondrial forms of Fumarase.		Fumarase deficiency is an autosomal recessive metabolic disorder distinguished by a deficiency of the enzyme Fumarate hydratase and indicated by an excess of Fumaric acid in the urine. It is common of infants with neurologic abnormalities and its potential causes include cytosolic and mitochondrial forms of Fumarase.
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