| Entry |
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| Name |
glucosamine-6-phosphate deaminase;
glucosaminephosphate isomerase;
glucosamine-6-phosphate isomerase;
phosphoglucosaminisomerase;
glucosamine phosphate deaminase;
aminodeoxyglucosephosphate isomerase;
phosphoglucosamine isomerase;
2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
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| Class |
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In other compounds
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| Sysname |
2-amino-2-deoxy-alpha-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
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| Reaction(IUBMB) |
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 [RN: R00765]
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| Reaction(KEGG) |
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| Substrate |
alpha-D-glucosamine 6-phosphate;
H2O [CPD: C00001]
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| Product |
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| Comment |
The enzyme uses ring opening and isomerization of the aldose-ketose type to convert the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.
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| History |
EC 3.5.99.6 created 1961 as EC 5.3.1.10, transferred 2000 to EC 3.5.99.6
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| Pathway |
| ec00520 | Amino sugar and nucleotide sugar metabolism |
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| Orthology |
| K02564 | glucosamine-6-phosphate deaminase |
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| Genes |
» show all
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| Reference |
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| Authors |
WOLFE JB, BRITTON BB, NAKADA HI. |
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| Title |
Glucosamine degradation by Escherichia coli. III. Isolation and studies of phosphoglucosaminisomerase. |
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| Journal |
Arch. Biochem. Biophys. 66 (1957) 333-9. |
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| Reference |
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| Authors |
COMB DG, ROSEMAN S. |
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| Title |
Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase. |
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| Journal |
J. Biol. Chem. 232 (1958) 807-27. |
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| Reference |
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| Authors |
PATTABIRAMAN TN, BACHHAWAT BK. |
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| Title |
Purification of glucosamine 6-phosphate deaminase from human brain. |
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| Journal |
Biochim. Biophys. Acta. 54 (1961) 273-83. |
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| Reference |
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| Authors |
Liu C, Li D, Liang YH, Li LF, Su XD |
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| Title |
Ring-opening mechanism revealed by crystal structures of NagB and its ES intermediate complex. |
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| Journal |
J. Mol. Biol. 379 (2008) 73-81. |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 3.5.99.6 |
| ExPASy - ENZYME nomenclature database: | 3.5.99.6 |
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