Formaldehyde dehydrogenase: Difference between revisions

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m Ubiquitous function: Journal cites:, added 1 PMC using AWB (10340)
 
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{{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>]].
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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 acceptorThe 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&ndash;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&ndash;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&ndash;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]]

Latest revision as of 10:16, 3 August 2014


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