Structural and Enzymatic Properties of 1-Aminocyclopropane-1-carboxylate Deaminase Homologue from Pyrococcus horikoshii

Fujino, Aiko; Ose, Toyoyuki; Yao, Ming; Tokiwano, Tetsuo; Honma, Mamoru; Watanabe, Nobuhisa; Tanaka, Isao

doi:10.1016/j.jmb.2004.06.062

Cited by 37 publications

(36 citation statements)

References 35 publications

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“…Structure prediction of the putative ACC deaminase from tomato, shown to lack this activity, was based on the availability of the 3D models of the yeast H. saturnus ACC deaminase (PDB ID # 1F2D) (Yao et al 2000), Pseudomonas sp. ACP ACC deaminase (PDB ID # 1TYZ) (Karthikeyan et al 2004b), as well as the Pyrococcus horikoshii ACC deaminase homolog PH0054 (PDB ID # 1J0A) (Fujino et al 2004). These potential templates were chosen with a BLAST search within the non-redundant SWISS-PROT Protein Sequence database and PDB database.…”

Section: Comparative Protein Modelingmentioning

confidence: 99%

“…From this data it has been calculated based on non-linear regression that the K i for AOA is 3.3 § 0.17 M. (Yao et al 2000;Karthikeyan et al 2004b). The structure of an ACC deaminase homolog from Pyrococcus horikoshii which lacks this activity, but is able to deaminate L-and D-serine has also been solved (PDB ID # 1J0A) (Fujino et al 2004). Based on these structures and mutagenesis studies, amino acid residues required for ACC deaminase activity have been identiWed (Honma 1985;Honma et al 1993;Yao et al 2000;Zhao and Liu 2002;Ose et al 2003;Zhao et al 2003;Fujino et al 2004;Karthikeyan et al 2004aKarthikeyan et al , 2004b.…”

Section: Protein Expression Puriwcation and Kinetic Characterizationmentioning

confidence: 99%

“…At these two positions the tomato D-cysteine desulfhydrase appears more like the P. horikoshii homolog of ACC deaminase and more like other members of the TRPS of PLP-dependent enzymes than a true ACC deaminase. Other members of TRPS are known to contain a serine or threonine residue at the position of Glu296; the side chain hydroxyl oxygen of serine or threonine hydrogen bonds with the nitrogen atom of the pyridinium ring of the co-factor, whereas the carboxylate oxygen of Glu296 has been shown to hydrogen bond with the nitrogen atom in ACC deaminase enzymes (Fujino et al 2004). The Leu323 residue of the H. saturnus ACC deaminase is thought to both provide space for the long side chain of glutamate (Glu296), as well as to stabilize the position of PLP within the active site (Fujino et al 2004).…”

Section: Protein Expression Puriwcation and Kinetic Characterizationmentioning

confidence: 99%

“…To gain insight into the functioning of this PLP-dependent enzyme, the crystal structures of bacterial (Pseudomonas sp. ACP) and yeast (H. saturnus) ACC deaminase and an ACC deaminase homolog without this activity from Pyrococcus horikoshii have been determined (Yao et al 2000;Ose et al 2003;Fujino et al 2004;Karthikeyan et al 2004b). The structures indicate that ACC deaminase belongs to the tryptophan synthase -subunit family (TRPS ) of PLP-dependent enzymes.…”

Section: Introductionmentioning

confidence: 99%

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The interconversion of ACC deaminase and d-cysteine desulfhydrase by directed mutagenesis

Todorović

Glick

2008

Planta

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Progress in DNA sequencing of plant genomes has revealed that, in addition to microorganisms, a number of plants contain genes which share similarity to microbial 1-aminocyclopropane-1-carboxylate (ACC) deaminases. These enzymes cleave ACC, the immediate precursor of ethylene in plants, into ammonia and alpha-ketobutyrate. We therefore sought to isolate putative ACC deaminase cDNAs from tomato plants with the objective of establishing whether the product of this gene is a functional ACC deaminase. In the work reported here, it was demonstrated that the enzyme encoded by the putative ACC deaminase cDNA does not have the ability to break the cyclopropane ring of ACC, but rather it utilizes D: -cysteine as a substrate, and in fact encodes a D: -cysteine desulfhydrase. Kinetic characterization of the tomato enzyme indicates that it is similar to other, previously characterized, D: -cysteine desulfhydrases. Using site-directed mutagenesis, it was shown that altering only two amino acid residues within the predicted active site served to change the enzyme from D: -cysteine desulfhydrase to ACC deaminase. Conversely, by altering two amino acid residues at the same positions within the active site of ACC deaminase from Pseudomonas putida UW4 the enzyme was converted into D: -cysteine desulfhydrase. Therefore, it is possible that a change in these two residues may have occurred in an ancestral protein to result in two different enzymatic activities.

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Section: Comparative Protein Modelingmentioning

confidence: 99%

Section: Protein Expression Puriwcation and Kinetic Characterizationmentioning

confidence: 99%

Section: Protein Expression Puriwcation and Kinetic Characterizationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The interconversion of ACC deaminase and d-cysteine desulfhydrase by directed mutagenesis

Todorović

Glick

2008

Planta

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“…Partial sequencing of the PCR products from strains HD9, HD110, HD125 and BMG1.7 showed identity between 97 and 99% to the B. cereus ATCC 14579 T accd gene. The high frequence of the presence of this gene could be explained by considering that this enzyme could be implicated in the deamination of substrates other than ACC as was found for the ACCD enzymes from Pseudomonas putida UW4 (Hontzeas et al, 2004) and Pyrococcus horikoshii (Fujino et al, 2004). Seven strains (HD22, BMG1.7, H77, H172, HD868, H156, H112) out of the 16 B. thuringiensis isolates tested were able to grow on DF mineral medium containing 3 mM of ACC as the sole nitrogen source as was shown by following the OD 600nm until 72 h of incubation (data not shown), and hence could have ACCD activity.…”

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confidence: 94%

Screening of plant growth promoting traits ofBacillus thuringiensis

et al. 2008

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-This study aimed to evaluate the plant growth promoting (PGP) potential of Bacillus thuringiensis. In this context, several genetic determinants of factors implicated in PGP potential were investigated by polymerase chain reaction (PCR) in 16 B. thuringiensis strains of different origin and belonging to different subspecies. PCR screening was performed on acid phosphatase, phytase, siderophore biosynthesis protein, 1-aminocyclopropane-1-carboxylate (ACC) deaminase and indolpyruvate decarboxylase (ipdC). Production of indol acetic acid (IAA)-like compounds and of ACC deaminase, and capability of solubilising mineral phosphate were investigated by phenotypic tests. All the strains were PCR positive for the presence of the siderophore biosynthesis protein, ACC deaminase and acid phosphatase genes. Five and seven strains gave an amplicon with the expected length for the phytase and ipdC genes respectively. All the strains produced IAA compounds and seven had a high capacity to solubilise inorganic phosphorous. Qualitative phenotypic test for ACC deaminase activity showed that seven strains are able to grow on salt minimal medium containing ACC as sole nitrogen source, indicating the expression of the accd genes. Our screening results in thirteen strains having more than one PGP trait and showed that B. thuringiensis harbours and expresses several PGP determinants that could be very interesting in field application to enhance the plant growth. To our knowledge, this is the first report on the multiple plant growth promoting potential of B. thuringiensis.

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Disruption of acdS gene reduces plant growth promotion activity and maize saline stress resistance by Rahnella aquatilis HX2

Peng

Liang

et al. 2019

J Basic Microbiol

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Rahnella aquatilis HX2 was isolated from Beijing vineyard soil and used as a plant growth‐promoting rhizobacterium in the field. Previous studies have shown that it has a broad in vitro antimicrobial spectrum and could inhibit a variety of plant pathogenic bacteria and fungi. In this study, a gene, acdS, encoding 1‐aminocyclopropane‐1‐carboxylic acid‐deaminase was disrupted by in‐frame deletion in the HX2 strain. Compared to the wild‐type, the acdS‐mutant had higher rates of nitrogen fixation, reduced indole‐3‐acetic acid production, lowered efficacy as a biological control agent against the grape crown gall pathogen Agrobacterium vitis. Under saline stress conditions, plant height, above‐ground fresh weight, root fresh weight of corn plants were increased by treatment with HX2 but this increase was compromised by the disruption of acdS gene. Our data confirmed the function of HX2 on plant growth promoting and demonstrated that acdS gene plays a major role in its PGPR activities.

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Structural and Enzymatic Properties of 1-Aminocyclopropane-1-carboxylate Deaminase Homologue from Pyrococcus horikoshii

Cited by 37 publications

References 35 publications

The interconversion of ACC deaminase and d-cysteine desulfhydrase by directed mutagenesis

The interconversion of ACC deaminase and d-cysteine desulfhydrase by directed mutagenesis

Screening of plant growth promoting traits ofBacillus thuringiensis

Disruption of acdS gene reduces plant growth promotion activity and maize saline stress resistance by Rahnella aquatilis HX2

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