RHEA:19105
| Enzymes help_outline | 1,479 proteins (UniProtKB) |
| Enzyme class help_outline |
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- Name help_outline 4-aminobutanal Identifier CHEBI:58264 Charge +1 Formula C4H10NO InChIKeyhelp_outline DZQLQEYLEYWJIB-UHFFFAOYSA-O SMILEShelp_outline [H]C(=O)CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 5,223 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 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_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 995 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-aminobutanoate Identifier CHEBI:59888 Charge 0 Formula C4H9NO2 InChIKeyhelp_outline BTCSSZJGUNDROE-UHFFFAOYSA-N SMILEShelp_outline [NH3+]CCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 19 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 InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 7,918 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 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILEShelp_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 963 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Links to other resources
| RHEA:19105 | RHEA:19106 | RHEA:19107 | RHEA:19108 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Citations
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Pyrrolidine and putrescine metabolism: gamma-aminobutyraldehyde dehydrogenase.
JAKOBY W.B., FREDERICKS J.
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Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase.
Gruez A., Roig-Zamboni V., Grisel S., Salomoni A., Valencia C., Campanacci V., Tegoni M., Cambillau C.
In the context of a medium-scaled structural genomics program aiming at solving the structures of as many as possible bacterial unknown open reading frame products from Escherichia coli (Y prefix), we have solved the structure of YdcW at 2.1A resolution, using molecular replacement. According to i ... >> More
In the context of a medium-scaled structural genomics program aiming at solving the structures of as many as possible bacterial unknown open reading frame products from Escherichia coli (Y prefix), we have solved the structure of YdcW at 2.1A resolution, using molecular replacement. According to its sequence identity, YdcW has been classified into the betaine aldehyde dehydrogenases family (EC 1.2.1.8), catalysing the oxidation of betaine aldehyde into glycine betaine. The structure of YdcW resembles that of other aldehyde dehydrogenases: it is tetrameric and binds a NADH molecule in each monomer. The NADH molecules, bound in the active site by soaking, are revealed to be in the "hydrolysis position". Activities experiments demonstrate that YdcW is more active on medium-chains aldehyde than on betaine aldehyde. However, soaking of betaine into YdcW crystals revealed its presence in one of the subunits, in two positions, a putative resting position and a hydride transfer ready position. Analysis of kinetics data and of the active site shape suggest an optimum binding of n-alkyl aldehydes up to seven to eight carbon atoms, possibly followed by a bulky cyclic or aromatic group. << Less
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Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase.
Samsonova N.N., Smirnov S.V., Novikova A.E., Ptitsyn L.R.
Gamma-aminobutyraldehyde dehydrogenase (ABALDH) from wild-type E. coli K12 was purified to apparent homogeneity and identified as YdcW by MS-analysis. YdcW exists as a tetramer of 202+/-29 kDa in the native state, a molecular mass of one subunit was determined as 51+/-3 kDa. Km parameters of YdcW ... >> More
Gamma-aminobutyraldehyde dehydrogenase (ABALDH) from wild-type E. coli K12 was purified to apparent homogeneity and identified as YdcW by MS-analysis. YdcW exists as a tetramer of 202+/-29 kDa in the native state, a molecular mass of one subunit was determined as 51+/-3 kDa. Km parameters of YdcW for gamma-aminobutyraldehyde, NAD+ and NADP+ were 41+/-7, 54+/-10 and 484+/-72 microM, respectively. YdcW is the unique ABALDH in E. coli K12. A coupling action of E. coli YgjG putrescine transaminase and YdcW dehydrogenase in vitro resulted in conversion of putrescine into gamma-aminobutyric acid. << Less
FEBS Lett. 579:4107-4112(2005) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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gamma-Guanidinobutyraldehyde Dehydrogenase of Vicia faba Leaves.
Matsuda H., Suzuki Y.
gamma-Guanidinobutyraldehyde dehydrogenase was purified 27-fold in 40% yield from extracts of Vicia faba leaves. High specificity exist only for gamma-guanidinobutyraldehyde and gamma-aminobutyraldehyde; the K(m) value was 3.4 micromolar for gamma-guanidinobutyraldehyde, 25 micromolar for gamma-am ... >> More
gamma-Guanidinobutyraldehyde dehydrogenase was purified 27-fold in 40% yield from extracts of Vicia faba leaves. High specificity exist only for gamma-guanidinobutyraldehyde and gamma-aminobutyraldehyde; the K(m) value was 3.4 micromolar for gamma-guanidinobutyraldehyde, 25 micromolar for gamma-aminobutyraldehyde, and 84 micromolar (case of gamma-guanidinobutyraldehyde) for NAD, respectively. The enzyme had a molecular weight of approximately 83,000. Optimal pH and temperature for activity were 9.5 and 45 degrees C, respectively. The enzyme was inhibited strongly by p-chloromercuribenzoate, N-ethylmaleimide, and zincon (2-carboxy-2'-hydroxy-5'-sulfoformazylbenzene). << Less
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A pathway for putrescine catabolism in Escherichia coli.
Prieto-Santos M.I., Martin-Checa J., Balana-Fouce R., Garrido-Pertierra A.
Escherichia coli mutants able to grow in putrescine have been isolated from gamma-aminobutyrate mutants. These mutants show putrescine-alpha-ketoglutarate transaminase and gamma-aminobutyraldehyde dehydrogenase activities. Both enzymes have been characterized, the first of them showing an apparent ... >> More
Escherichia coli mutants able to grow in putrescine have been isolated from gamma-aminobutyrate mutants. These mutants show putrescine-alpha-ketoglutarate transaminase and gamma-aminobutyraldehyde dehydrogenase activities. Both enzymes have been characterized, the first of them showing an apparent Km for putrescine of 22.5 microM and the second an apparent Km of 37 microM for NAD and 18 microM for delta-1-pyrroline; the optimum pH values were 7.2 and 5.4, respectively, for the two enzymes. << Less
Biochim. Biophys. Acta 880:242-244(1986) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Purification and properties of 4-aminobutanal dehydrogenase from a Pseudomonas species.
Callewaert D.M., Rosemblatt M.S., Tchen T.T.