Formaldehyde dehydrogenase - Revision history

en>Rjwilmsi: /* Ubiquitous function */Journal cites:, added 1 PMC using AWB (10340)

2014-08-03T08:16:57Z

Ubiquitous function: Journal cites:, added 1 PMC using AWB (10340)

← Older revision		Revision as of 10:16, 3 August 2014
Line 1:		Line 1:
	~~{{enzyme~~
	~~\| Name = glutamyl-tRNA reductase~~
	~~\| EC_number = 1.2.1.70~~
	~~\| CAS_number =~~
	~~\| IUBMB_EC_number = 1/2/1/70~~
	~~\| GO_code = 0008883~~
	~~\| image =~~
	~~\| width =~~
	~~\| caption =~~
	}}
	~~A '''glutamyl-tRNA reductase''' ({{EC number\|1.2.1.70}}) is an [[enzyme]] that [[catalysis\|catalyzes]] the [[chemical reaction]]~~

	~~:L-glutamate 1-semialdehyde + NADP<sup>+</sup> + tRNAGlu <math>\rightleftharpoons</math> L-glutamyl-tRNAGlu + NADPH + H<sup>+</sup>~~

	The 3 [[substrate (biochemistry)\|substrates]] of this enzyme are [[L-glutamate 1-semialdehyde]], [[nicotinamide adenine dinucleotide phosphate\|NADP<sup>+</sup>]], and [[tRNA(Glu)]], whereas its 3 [[product (chemistry)\|products]] are [[L-glutamyl-tRNA(Glu)]], [[nicotinamide adenine dinucleotide phosphate\|NADPH]], and [[hydrogen ion\|H<sup>+</sup>]].		The author's name is Steve Larsen when people use his name but he doesn't like,. Michigan is where she reside but now she is considering additional options She was previously unemployed but quickly she'll be on her own although now he's a library helper. One of many issues I enjoy most will be to gather kites and that I could not give it-up Goto my site to find out more: http://www.againcollection.com/<br><br>My web page :: [http://www.againcollection.com/ timeless apparel]

	~~This enzyme belongs to the family of [[oxidoreductase]]~~s, ~~to be specific, those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor~~. ~~The systematic name of this enzyme class~~ is ''~~'L-glutamate-semialdehyde: NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming)'''. This enzyme participates in [[porphyrin]] and [[chlorophyll]] metabolism~~.

	~~==References==~~
	~~{{reflist\|1}}~~
	* {{cite journal \| author = Von Wettstein D, Gough S, Kannangara CG \| date = 1995 \| title = Chlorophyll Biosynthesis \| journal = Plant. Cell. \| volume = 7 \| pages = 1039–1057 \| pmid = 12242396 \| doi = 10.1105/tpc.7.7.1039 \| issue = 7 \| pmc = 160907 }}
	* {{cite journal \| author = Pontoppidan B, Kannangara CG \| date = 1994 \| title = Purification and ~~partial characterisation of barley glutamyl~~-~~tRNA(Glu) reductase, the enzyme that directs glutamate~~ to ~~chlorophyll biosynthesis \| journal = Eur. J. Biochem. \| volume = 225 \| pages = 529–37 \| pmid = 7957167 \| doi = 10.1111~~/~~j.1432-1033.1994.00529.x \| issue = 2 }}~~
	* {{cite journal \| author = Heinz DW, Inokuchi H, Soll D, Jahn D \| date = 2002 \| title = Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate \| journal = J. ~~Biol~~. ~~Chem. \| volume = 277 \| pages = 48657–63 \| pmid = 12370189 \| doi = 10.1074~~/~~jbc.M206924200 \| issue = 50 }}~~

	~~{{1.2-enzyme-stub}}~~

	[[~~Category~~:~~EC 1~~.2.~~1]]~~
	~~[[Category:NADPH-dependent enzymes]]~~
	~~[[Category:Enzymes of unknown structure]~~]

en>Monkbot: Fix CS1 deprecated date parameter errors

2014-01-19T00:45:46Z

Fix CS1 deprecated date parameter errors

← Older revision		Revision as of 02:45, 19 January 2014
Line 1:		Line 1:
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Some people consider they may be protecting unhealthy calories by missing your morning meal. 1 purposе this doesn't work is it making you more pгone~~ to go for treats for your craving for food builds. 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Being familiar with diet and exactly how it has an effect on you is esѕential to keep healthful and residе and long life.~~		{{enzyme
			\| Name = glutamyl-tRNA reductase
			\| EC_number = 1.2.1.70
			\| CAS_number =
			\| IUBMB_EC_number = 1/2/1/70
			\| GO_code = 0008883
			\| image =
			\| width =
			\| caption =
			}}
			A '''glutamyl-tRNA reductase''' ({{EC number\|1.2.1.70}}) is an [[enzyme]] that [[catalysis\|catalyzes]] the [[chemical reaction]]

			:L-glutamate 1-semialdehyde + NADP<sup>+</sup> + tRNAGlu <math>\rightleftharpoons</math> L-glutamyl-tRNAGlu + NADPH + H<sup>+</sup>

			The 3 [[substrate (biochemistry)\|substrates]] of this enzyme are [[L-glutamate 1-semialdehyde]], [[nicotinamide adenine dinucleotide phosphate\|NADP<sup>+</sup>]], and [[tRNA(Glu)]], whereas its 3 [[product (chemistry)\|products]] are [[L-glutamyl-tRNA(Glu)]], [[nicotinamide adenine dinucleotide phosphate\|NADPH]], and [[hydrogen ion\|H<sup>+</sup>]].

			This enzyme belongs to the family of [[oxidoreductase]]s, to be specific, those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is '''L-glutamate-semialdehyde: NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming)'''. This enzyme participates in [[porphyrin]] and [[chlorophyll]] metabolism.

			==References==
			{{reflist\|1}}
			* {{cite journal \| author = Von Wettstein D, Gough S, Kannangara CG \| date = 1995 \| title = Chlorophyll Biosynthesis \| journal = Plant. Cell. \| volume = 7 \| pages = 1039–1057 \| pmid = 12242396 \| doi = 10.1105/tpc.7.7.1039 \| issue = 7 \| pmc = 160907 }}
			* {{cite journal \| author = Pontoppidan B, Kannangara CG \| date = 1994 \| title = Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis \| journal = Eur. J. Biochem. \| volume = 225 \| pages = 529–37 \| pmid = 7957167 \| doi = 10.1111/j.1432-1033.1994.00529.x \| issue = 2 }}
			* {{cite journal \| author = Heinz DW, Inokuchi H, Soll D, Jahn D \| date = 2002 \| title = Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate \| journal = J. Biol. Chem. \| volume = 277 \| pages = 48657–63 \| pmid = 12370189 \| doi = 10.1074/jbc.M206924200 \| issue = 50 }}

			{{1.2-enzyme-stub}}

			[[Category:EC 1.2.1]]
			[[Category:NADPH-dependent enzymes]]
			[[Category:Enzymes of unknown structure]]

en>Sun Creator: Typo fixing, General and delinking, typos fixed: et al → et al. using AWB

2012-06-21T10:13:39Z

Typo fixing, General and delinking, typos fixed: et al → et al. using AWB

New page

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