The Enzyme Database

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EC 1.5.1.19     
Accepted name: D-nopaline dehydrogenase
Reaction: N2-(D-1,3-dicarboxypropyl)-L-arginine + NADP+ + H2O = L-arginine + 2-oxoglutarate + NADPH + H+
Other name(s): D-nopaline synthase; nopaline dehydrogenase; nopaline synthase; NOS; 2-N-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase (L-arginine-forming)
Systematic name: N2-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase (L-arginine-forming)
Comments: In the reverse direction, forms D-nopaline from L-arginine and D-ornaline from L-ornithine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64763-57-1
References:
1.  Kemp, J.D., Sutton, D.W. and Hack, E. Purification and characterization of the crown gall specific enzyme nopaline synthase. Biochemistry 18 (1979) 3755–3760. [PMID: 476084]
[EC 1.5.1.19 created 1984]
 
 
EC 3.6.3.21      
Transferred entry: polar-amino-acid-transporting ATPase. Now EC 7.4.2.1, ABC-type polar-amino-acid transporter
[EC 3.6.3.21 created 2000, deleted 2018]
 
 
EC 7.4.2.1     
Accepted name: ABC-type polar-amino-acid transporter
Reaction: ATP + H2O + polar amino acid-[polar amino acid-binding protein][side 1] = ADP + phosphate + polar amino acid[side 2] + [polar amino acid-binding protein][side 1]
Glossary: nopaline = N-{(1R)-1-carboxy-4-[(diaminomethylene)amino]butyl}-L-glutamate
Other name(s): histidine permease; polar-amino-acid-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, polar-amino-acid-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of polar amino acids. This entry comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
2.  Nikaido, K., Liu, P.Q. and Ferro-Luzzi Ames, G. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubilization, dimerization , and ATPase activity. J. Biol. Chem. 272 (1997) 27745–27752. [DOI] [PMID: 9346917]
3.  Walshaw, D.L., Lowthorpe, S., East, A. and Poole, P.S. Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity. FEBS Lett. 414 (1997) 397–401. [DOI] [PMID: 9315727]
4.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
[EC 7.4.2.1 created 2000 as EC 3.6.3.21, transferred 2018 to EC 7.4.2.1]
 
 


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