Rhea - reaction knowledgebase

Enzymes

Enzyme class ^help_outline	EC 1.1.1.114 apiose 1-reductase
GO Molecular Function ^help_outline	GO:0047674 apiose 1-reductase activity

Reaction participants Show >> << Hide

Name ^help_outline D-apiitol Identifier CHEBI:17702 (Beilstein: 4242143; CAS: 10592-17-3) ^help_outline Charge 0 Formula C5H12O5 InChIKey^help_outline SDXWEZQDLHNYFR-BYPYZUCNSA-N SMILES^help_outline OC[C@H](O)C(O)(CO)CO 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline NAD⁺ Identifier CHEBI:57540 (Beilstein: 3868403) ^help_outline Charge -1 Formula C21H26N7O14P2 InChIKey^help_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILES^help_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline aldehydo-D-apiose Identifier CHEBI:16689 (CAS: 639-97-4) ^help_outline Charge 0 Formula C5H10O5 InChIKey^help_outline AVGPOAXYRRIZMM-BYPYZUCNSA-N SMILES^help_outline OCC(O)(CO)[C@@H](O)C=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) ^help_outline Charge -2 Formula C21H27N7O14P2 InChIKey^help_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILES^help_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,073 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:15301	RHEA:15302	RHEA:15303	RHEA:15304
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline
EC numbers ^help_outline	1.1.1.114
Gene Ontology ^help_outline	GO:0047674
KEGG ^help_outline				R03577
MetaCyc ^help_outline			APIOSE-1-REDUCTASE-RXN

Publications

D-apiose reductase from Aerobacter aerogenes.

Neal D.L., Kindel P.K.

A strain of Aerobacter aerogenes PRL-R3 has been isolated which utilizes d-apiose as its sole source of carbon. A new enzyme, d-apiose reductase, was discovered in this strain. The enzyme was not present when the strain was grown on d-glucose. d-Apiose reductase catalyzes the nicotinamide adenine ... >> More

A strain of Aerobacter aerogenes PRL-R3 has been isolated which utilizes d-apiose as its sole source of carbon. A new enzyme, d-apiose reductase, was discovered in this strain. The enzyme was not present when the strain was grown on d-glucose. d-Apiose reductase catalyzes the nicotinamide adenine dinucleotide-dependent interconversion of d-apiose and d-apiitol. The enzyme is specific for d-apiose and d-apiitol, with a few possible exceptions. The K(m) for d-apiose is 0.02 m. The K(m) for d-apiitol is 0.01 m. The enzyme is almost completely specific for the reduced and oxidized forms of nicotinamide adenine dinucleotide. When cell-free extracts were centrifuged at 100,000 x g for 1 hr, the enzyme remained in solution. Optimal activity for the reduction of d-apiose was obtained at pH 7.5 in glycylglycine buffer, whereas for the oxidation of d-apiitol it was obtained at pH 10.5 in glycine buffer. Enzymatic reduction of d-apiose was not appreciably affected by the presence of 0.02 m ethylenediaminetetraacetate. Paper chromatography and specific spray reagents were used to identify d-apiitol and d-apiose as the products of this reversible reaction. d-Apiose and d-apiitol did not serve as substrates for ribitol dehydrogenase and d-arabitol dehydrogenase from A. aerogenes PRL-R3. << Less

J Bacteriol 101:910-915(1970) [PubMed] [EuropePMC]

Comments

Published in: Hanna, R., Picken, M. and Mendicino, J. Purification of a specific D-apiitol dehydrogenase from a Micrococcus isolated from the surface of germinating parsley. Biochim. Biophys. Acta 315 (1973) 259–271.