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{{enzyme
| Name = glucosamine-6-phosphate deaminase
| EC_number = 3.5.99.6
| CAS_number = 9013-10-9
| IUBMB_EC_number = 3/5/99/6
| GO_code = 0004342
| image =
| width =
| caption =
}}
In [[enzymology]], a '''glucosamine-6-phosphate deaminase''' ({{EC number|3.5.99.6}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]


:D-glucosamine 6-phosphate + H<sub>2</sub>O <math>\rightleftharpoons</math> D-fructose 6-phosphate + NH<sub>3</sub>


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Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[glucosamine 6-phosphate]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[fructose 6-phosphate]] and [[ammonia|NH<sub>3</sub>]].
 
This enzyme belongs to the family of [[hydrolase]]s, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is '''2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)'''. Other names in common use include '''glucosaminephosphate isomerase''', '''glucosamine-6-phosphate isomerase''', '''phosphoglucosaminisomerase''', '''glucosamine phosphate deaminase''', '''aminodeoxyglucosephosphate isomerase''', and '''phosphoglucosamine isomerase'''. This enzyme participates in [[aminosugars metabolism]]. This enzyme has at least one [[effector (biology)|effector]], [[N-Acetyl-D-glucosamine 6-phosphate]].
 
==Structural studies==
 
As of late 2007, 5 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1J5X}}, {{PDB link|1JT9}}, {{PDB link|1NE7}}, {{PDB link|2BKV}}, and {{PDB link|2BKX}}.
 
==References==
{{reflist|1}}
* {{cite journal | author = COMB DG, ROSEMAN S | year = 1958 | title = Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase | journal = J. Biol. Chem. | volume = 232 | pages = 807&ndash;27  | pmid = 13549465 | issue = 2 }}
* {{cite journal | author = Pattabiraman TN, Bachhawat BK | year = 1961 | title = Purification of glucosamine 6-phosphate deaminase from human brain | journal = Biochim. Biophys. Acta  | volume = 54 | pages = 273&ndash;283 | doi = 10.1016/0006-3002(61)90366-3 | pmid=14484386 | issue = 2}}
* {{cite journal | author = Wolfe JB, Britton BB, Nakada HI | year = 1957 | title = Glucosamine degradation by Escherichia coli. III. Isolation and studies of "phosphoglucosaminisomerase" | journal = Arch. Biochem Biophys. | volume = 66 | pages = 333&ndash;339 | doi = 10.1016/S0003-9861(57)80008-3 | issue = 2 }}
 
[[Category:EC 3.5.99]]
[[Category:Enzymes of known structure]]
 
 
{{hydrolase-stub}}

Latest revision as of 22:42, 11 May 2013

Template:Enzyme In enzymology, a glucosamine-6-phosphate deaminase (Air Transportation Experts Kull from Wingham, has many interests that include butterflies, property developers in singapore and digital photography. Is a travel freak and in recent past made buy a house in singapore journey to Paleochristian and Byzantine Monuments of Thessalonika.) is an enzyme that catalyzes the chemical reaction

D-glucosamine 6-phosphate + H2O D-fructose 6-phosphate + NH3

Thus, the two substrates of this enzyme are glucosamine 6-phosphate and H2O, whereas its two products are fructose 6-phosphate and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing). Other names in common use include glucosaminephosphate isomerase, glucosamine-6-phosphate isomerase, phosphoglucosaminisomerase, glucosamine phosphate deaminase, aminodeoxyglucosephosphate isomerase, and phosphoglucosamine isomerase. This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, N-Acetyl-D-glucosamine 6-phosphate.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, and Template:PDB link.

References

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  • One of the biggest reasons investing in a Singapore new launch is an effective things is as a result of it is doable to be lent massive quantities of money at very low interest rates that you should utilize to purchase it. Then, if property values continue to go up, then you'll get a really high return on funding (ROI). Simply make sure you purchase one of the higher properties, reminiscent of the ones at Fernvale the Riverbank or any Singapore landed property Get Earnings by means of Renting

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    There are various methods to go about discovering the precise property. Some local newspapers (together with the Straits Instances ) have categorised property sections and many local property brokers have websites. Now there are some specifics to consider when buying a 'new launch' rental. Intended use of the unit Every sale begins with 10 p.c low cost for finish of season sale; changes to 20 % discount storewide; follows by additional reduction of fiftyand ends with last discount of 70 % or extra. Typically there is even a warehouse sale or transferring out sale with huge mark-down of costs for stock clearance. Deborah Regulation from Expat Realtor shares her property market update, plus prime rental residences and houses at the moment available to lease Esparina EC @ Sengkang
  • One of the biggest reasons investing in a Singapore new launch is an effective things is as a result of it is doable to be lent massive quantities of money at very low interest rates that you should utilize to purchase it. Then, if property values continue to go up, then you'll get a really high return on funding (ROI). Simply make sure you purchase one of the higher properties, reminiscent of the ones at Fernvale the Riverbank or any Singapore landed property Get Earnings by means of Renting

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Template:Hydrolase-stub