The Enzyme Database

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EC 2.7.1.203     
Accepted name: protein-Nπ-phosphohistidine—D-glucosaminate phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + 2-amino-2-deoxy-D-gluconate[side 1] = [protein]-L-histidine + 2-amino-2-deoxy-D-gluconate 6-phosphate[side 2]
Other name(s): dgaABCD (gene names); 2-amino-2-deoxy-D-gluconate PTS permease
Systematic name: protein-Nπ-phospho-L-histidine:2-amino-2-deoxy-D-gluconate Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Miller, K.A., Phillips, R.S., Mrazek, J. and Hoover, T.R. Salmonella utilizes D-glucosaminate via a mannose family phosphotransferase system permease and associated enzymes. J. Bacteriol. 195 (2013) 4057–4066. [DOI] [PMID: 23836865]
[EC 2.7.1.203 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.203]
 
 
EC 4.3.1.9     
Accepted name: glucosaminate ammonia-lyase
Reaction: 2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate + NH3 (overall reaction)
(1a) 2-amino-2-deoxy-D-gluconate = (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate + H2O
(1b) (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate = (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate (spontaneous)
(1c) (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate + H2O = 2-dehydro-3-deoxy-D-gluconate + NH3 (spontaneous)
Glossary: 2-amino-2-deoxy-D-gluconate = glucosaminate
Other name(s): glucosaminic dehydrase; D-glucosaminate dehydratase; D-glucosaminic acid dehydrase; aminodeoxygluconate dehydratase; 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating); aminodeoxygluconate ammonia-lyase; 2-amino-2-deoxy-D-gluconate ammonia-lyase; D-glucosaminate ammonia-lyase; D-glucosaminate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming)
Systematic name: 2-amino-2-deoxy-D-gluconate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming)
Comments: Contains pyridoxal phosphate. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination to form the final product.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-91-8
References:
1.  Imanaga, Y. Metabolism of D-glucosamine. III. Enzymic degradation of D-glucosaminic acid. J. Biochem. (Tokyo) 45 (1958) 647–650.
2.  Merrick, J.M. and Roseman, S. D-Glucosaminic acid dehydrase. Methods Enzymol. 9 (1966) 657–660.
3.  Iwamoto, R., Imanaga, Y. and Soda, K. D-Glucosaminate dehydratase from Agrobacterium radiobacter. Physicochemical and enzymological properties. J. Biochem. (Tokyo) 91 (1982) 283–289. [PMID: 7068563]
4.  Iwamoto, R., Taniki, H., Koishi, J. and Nakura, S. D-Glucosaminate aldolase activity of D-glucosaminate dehydratase from Pseudomonas fluorescens and its requirement for Mn2+ ion. Biosci. Biotechnol. Biochem. 59 (1995) 408–411. [DOI] [PMID: 7766176]
[EC 4.3.1.9 created 1972, (EC 4.3.1.21 created 1965 as EC 4.2.1.26, transferred 2002 to EC 4.3.1.21, incorporated 2004) modified 2004]
 
 
EC 4.3.1.29     
Accepted name: D-glucosaminate-6-phosphate ammonia-lyase
Reaction: 2-amino-2-deoxy-D-gluconate 6-phosphate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + NH3
Other name(s): DgaE; 6-phospho-D-glucosaminate ammonia-lyase (2-dehydro-3-deoxy-6-phospho-D-gluconate-forming)
Systematic name: 2-amino-2-deoxy-D-gluconate 6-phosphate ammonia-lyase (2-dehydro-3-deoxy-6-phospho-D-gluconate-forming)
Comments: The enzyme, from the bacterium Salmonella typhimurium, is involved in the degradation pathway of 2-amino-2-deoxy-D-gluconate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Miller, K.A., Phillips, R.S., Mrazek, J. and Hoover, T.R. Salmonella utilizes D-glucosaminate via a mannose family phosphotransferase system permease and associated enzymes. J. Bacteriol. 195 (2013) 4057–4066. [DOI] [PMID: 23836865]
[EC 4.3.1.29 created 2013]
 
 


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