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4.3.1.9 |
| Description |
Glucosaminate ammonia-lyase. |
| Alternative names |
2-amino-2-deoxy-D-gluconate ammonia-lyase.
2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating).
Acetylenemonocarboxylic acid hydrase.
Aminodeoxygluconate ammonia-lyase.
Aminodeoxygluconate dehydratase.
D-glucosaminate dehydratase.
D-glucosaminic acid dehydrase.
Glucosaminic dehydrase.
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| Catalyzed reaction |
D-glucosaminate = 2-dehydro-3-deoxy-D-gluconate + NH(3). |
| Cofactor |
Pyridoxal-phosphate. |
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The enzyme from Pseudomonas fluorescens reportedly encompasses two types of subunits (alpha and beta). The alpha-subunit was sequenced and found highly similar to several thioredoxin reductases (TrxR) from bacteria. |
| Organisms |
-Eubacteria -Bacteria |
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| Links |
Enzyme (activities) 4.3.1.9
BRENDA (activities) 4.3.1.9
KEGG (pathways) 4.3.1.9
PLPMDB (PLP mutants) 4.3.1.9
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| References |
Iwamoto R, Amano C, Ikehara K, Ushida N. (2003) The D-glucosaminate dehydratase alpha-subunit from Pseudomonas fluorescens exhibits thioredoxin reductase activity Biochim Biophys Acta 1647 310-4. Iwamoto, R.; Taniki, H.; Koishi, J.; Nakura, S. (1995) D-glucosaminate aldolase activity of D-glucosaminate dehydratase from Pseudomonas fluorescens and its requirement for Mn2+ ion Biosci Biotechnol Biochem 59 408-11.. Iwamoto, R.; Imanaga, Y.; Soda, K. (1982) D-glucosaminate dehydratase from Agrobacterium radiobacter. Physicochemical and enzymological properties J Biochem (Tokyo) 91 283-9.. |
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| last changed |
2007/12/17 16:55 |
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