Monovalent cations requirements for the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, porcine kidney and amaranth leaves

Valenzuela‐Soto, Elisa M.; Velasco-Garcı́a, Roberto; Mújica-Jiménez, Carlos; Gaviria-González, L Laraí; Muñoz‐Clares, Rosario A.

doi:10.1016/s0009-2797(02)00198-9

Cited by 37 publications

(28 citation statements)

References 27 publications

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“…Curiously, in a recent paper, Gonzáles-Segura and coauthors (25) suggested that this "crystallographic water" molecule bound at the C terminus of helix G could be a potassium atom. Located in the inter-subunit interface, this atom seems to be critical for maintaining the tetrameric state of Pseudomonas aeruginosa betaine ALDH (44). The authors proposed that binding of a stabilizing potassium or sodium atom at this position could be a general feature of ALDH.…”

Section: Discussionmentioning

confidence: 99%

Conserved Catalytic Residues of the ALDH1L1 Aldehyde Dehydrogenase Domain Control Binding and Discharging of the Coenzyme

Tsybovsky¹,

Krupenko

2011

Journal of Biological Chemistry

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The C-terminal domain (C t -FDH) of 10-formyltetrahydrofolate dehydrogenase (FDH, ALDH1L1) is an NADP ؉ -dependent oxidoreductase and a structural and functional homolog of aldehyde dehydrogenases. Here we report the crystal structures of several C t -FDH mutants in which two essential catalytic residues adjacent to the nicotinamide ring of bound NADP ؉ , Cys-707 and Glu-673, were replaced separately or simultaneously. The replacement of the glutamate with an alanine causes irreversible binding of the coenzyme without any noticeable conformational changes in the vicinity of the nicotinamide ring. Additional replacement of cysteine 707 with an alanine (E673A/ C707A double mutant) did not affect this irreversible binding indicating that the lack of the glutamate is solely responsible for the enhanced interaction between the enzyme and the coenzyme. The substitution of the cysteine with an alanine did not affect binding of NADP ؉ but resulted in the enzyme lacking the ability to differentiate between the oxidized and reduced coenzyme: unlike the wild-type C t -FDH/NADPH complex, in the C707A mutant the position of NADPH is identical to the position of NADP ؉ with the nicotinamide ring well ordered within the catalytic center. Thus, whereas the glutamate restricts the affinity for the coenzyme, the cysteine is the sensor of the coenzyme redox state. These conclusions were confirmed by coenzyme binding experiments. Our study further suggests that the binding of the coenzyme is additionally controlled by a longrange communication between the catalytic center and the coenzyme-binding domain and points toward an ␣-helix involved in the adenine moiety binding as a participant of this communication.Enzymes belonging to the family of aldehyde dehydrogenases (ALDH) 3 are involved in conversions of a broad variety of aliphatic and aromatic aldehydes to their respective carboxylic acids (1-3). These enzymes are either dimers or tetramers of identical subunits (1). Numerous crystal structures showed that subunits of different ALDHs have very similar fold with each composed of catalytic, nucleotide binding, and oligomerization domains (4 -10).Two members of the family, cytosolic ALDH1 and mitochondrial ALDH2, are essential components of the pathway metabolizing ethanol (2, 11). ALDH2 is also involved in mediating the vasodilator activity of nitroglycerine (12). Furthermore, activation of this enzyme correlates with reduced ischemic heart damage in rodent models (13). The polymorphism in the ALDH2 gene found in about 40% of the Asian population causes decreased tolerance to alcohol in heterozygous and homozygous individuals (14). This ALDH2 genetic variant, ALDH2 * 2, has a lysine instead of a glutamate at position 487 within the oligomerization domain of the tetrameric enzyme. This substitution induces conformational changes at the subunit interface, which are reflected by structural alterations within the catalytic center and the coenzyme binding site (5, 15, 16). The final outcome is a strong decrease in the affinity for NAD ...

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Section: Discussionmentioning

confidence: 99%

Conserved Catalytic Residues of the ALDH1L1 Aldehyde Dehydrogenase Domain Control Binding and Discharging of the Coenzyme

Tsybovsky¹,

Krupenko

2011

Journal of Biological Chemistry

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“…Enzyme assay mixtures (1 ml total volume) were based on the work of Yorifuji et al (1986), Trossat et al (1997), Valenzuela-Soto et al (2003) and Oishi and Ebina (2005) and contained 50 mM HEPES, MES or Glycine Buffer, 20 mM b-mercaptoethanol, 2 mM NAD+, with 10 ug of enzyme (BAD1 or BAD2) and varying concentrations of substrates. HEPES and MES buffers were obtained from Sigma, glycine buffer consisted of 50 mM glycine, 1 mM MgSO 4 , 0.1 mM ZnSO 4 .…”

Section: Enzyme Assaymentioning

confidence: 99%

Inactivation of an aminoaldehyde dehydrogenase is responsible for fragrance in rice

et al. 2008

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Rice (Oryza sativa) has two betaine aldehyde dehydrogenase homologs, BAD1 and BAD2, encoded on chromosome four and chromosome eight respectively. BAD2 is responsible for the characteristic aroma of fragrant rice. Complementary DNA clones of both BAD1 and BAD2 were isolated and expressed in E. coli. BAD2 had optimum activity at pH 10, little to no affinity towards Nacetyl-c-aminobutyraldehyde (NAGABald) with a Km of approximately 10 mM and moderate affinity towards c-guanidinobutyraldehyde (GGBald) and betaine aldehyde (bet-ald) with Km values of approximately 260 lM and 63 lM respectively. A lower Km of approximately 9 lM was observed with c-aminobutyraldehyde (GABald), suggesting BAD2 has a higher affinity towards this substate in vivo. The enzyme encoded on chromosome four, BAD1, had optimum activity at pH 9.5, showed little to no affinity towards bet-ald with a Km of 3 mM and had moderate affinity towards GGBald, NAGABald and GABald with Km values of approximately 545, 420 and 497 lM respectively. BAD1 had a half life roughly double that of BAD2. We discuss the implications of these findings on the pathway of fragrance generation in Basmati and Jasmine rice and the potential of rice to accumulate the osmoprotectant glycine betaine.

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“…However, the addition of 1 mM Mn 2+ and Mg 2+ enhanced its activity by 21% and 19%, respectively (Table 3). The improvement of enzyme activity may be attributed to keeping the stability of enzymatic quaternary structure by metal ions, or a steric interaction between the metal ions and the key amino acids related (Ho et al, 2005;Valenzuela et al, 2003).…”

Section: Biochemical Properties Of the C Glutamicum Phenol Hydroxylasementioning

confidence: 99%

Molecular characterization of a eukaryotic-like phenol hydroxylase from <i>Corynebacterium glutamicum</i>

Xiao

Zhong

et al. 2015

J. Gen. Appl. Microbiol.

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Monovalent cations requirements for the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, porcine kidney and amaranth leaves

Cited by 37 publications

References 27 publications

Conserved Catalytic Residues of the ALDH1L1 Aldehyde Dehydrogenase Domain Control Binding and Discharging of the Coenzyme

Conserved Catalytic Residues of the ALDH1L1 Aldehyde Dehydrogenase Domain Control Binding and Discharging of the Coenzyme

Inactivation of an aminoaldehyde dehydrogenase is responsible for fragrance in rice

Molecular characterization of a eukaryotic-like phenol hydroxylase from <i>Corynebacterium glutamicum</i>

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