Characterization of the <i>Rhodococcus</i> sp. BPG‐8 resorcinol hydroxylase

Armstrong, S. M.; Patel, Thakor R.

doi:10.1002/jobm.3620330202

Cited by 3 publications

(2 citation statements)

References 13 publications

(5 reference statements)

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“…In contrast to the findings for the M glycoprotein of IBV, Machamer et al [90] have shown that the first transmembrane domain of the M glycoprotein of the related murine coronavirus mouse hepatitis virus (MHV) is not sufficient for Golgi localization. Indeed, Armstrong and Patel [92] had earlier reported that the MHV M glycoprotein requires its cytoplasmic tail for Golgi retention. However, these investigators also noted that alterations of other domains of native MHV M protein were found to perturb Golgi localization.…”

Section: Golgi-localized Viral Proteinsmentioning

confidence: 99%

Targeting of proteins to the Golgi apparatus

1994

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The Golgi apparatus maintains a highly organized structure in spite of the intense membrane traffic which flows into and out of this organelle. Resident Golgi proteins must have localization signals to ensure that they are targeted to the correct Golgi compartment and not swept further along the secretory pathway. There are a number of distinct groups of Golgi membrane proteins, including glycosyltransferases, recycling trans-Golgi network proteins, peripheral membrane proteins, receptors and viral glycoproteins. Recent studies indicate that there are a number of different Golgi localization signals and mechanisms for retaining proteins to the Golgi apparatus. This review focuses on the current knowledge in this field.

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Section: Golgi-localized Viral Proteinsmentioning

confidence: 99%

Targeting of proteins to the Golgi apparatus

1994

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“…The relatively high K d (FAD) of 2.8 M for the Azotobacter enzyme compared to values from 0.039 to 0.28 M for other monooxygenases (1,3,20) suggests that FAD is a loosely bound cofactor. The total amount of FAD is lost during enzyme purification, and the loss is probably enhanced by the presence of high salt concentrations.…”

Section: Discussionmentioning

confidence: 91%

Purification and characterization of 2,4,6-trichlorophenol-4-monooxygenase, a dehalogenating enzyme from Azotobacter sp. strain GP1

et al. 1997

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The enzyme which catalyzes the dehalogenation of 2,4,6-trichlorophenol (TCP) was purified to apparent homogeneity from an extract of TCP-induced cells of Azotobacter sp. strain GP1. The initial step of TCP degradation in this bacterium is inducible by TCP; no activity was found in succinate-grown cells or in phenol-induced cells. NADH, flavin adenine dinucleotide, and O 2 are required as cofactors. As reaction products, 2,6-dichlorohydroquinone and Cl ؊ ions were identified. Studies of the stoichiometry revealed the consumption of 2 mol of NADH plus 1 mol of O 2 per mol of TCP and the formation of 1 mol of Cl ؊ ions. No evidence for membrane association or for a multicomponent system was obtained. Molecular masses of 240 kDa for the native enzyme and 60 kDa for the subunit were determined, indicating a homotetrameric structure. Cross-linking studies with dimethylsuberimidate were consistent with this finding. TCP was the best substrate for 2,4,6-trichlorophenol-4-monooxygenase (TCP-4-monooxygenase). The majority of other chlorophenols converted by the enzyme bear a chloro substituent in the 4-position. 2,6-Dichlorophenol, also accepted as a substrate, was hydroxylated in the 4-position to 2,6-dichlorohydroquinone in a nondehalogenating reaction. NADH and O 2 were consumed by the pure enzyme also in the absence of TCP with simultaneous production of H 2 O 2 . The NH 2 -terminal amino acid sequence of TCP-4-monooxygenase from Azotobacter sp. strain GP1 revealed complete identity with the nucleotide-derived sequence from the analogous enzyme from Pseudomonas pickettii and a high degree of homology with two nondehalogenating monooxygenases. The similarity in enzyme properties and the possible evolutionary relatedness of dehalogenating and nondehalogenating monooxygenases are discussed.Polychlorinated phenols are widespread environmental pollutants, and their degradation has been the subject of numerous investigations (for reviews, see references 5, 9, 10, and 21). While many different microorganisms with the capacity to degrade these compounds have been isolated, relatively few reports have dealt with the initial step of their degradation. Moreover, the majority of these investigations were performed with whole cells, crude extracts, or partially purified enzymes, and so far only two polychlorophenol-dehalogenating enzymes from Burkholderia (formerly Pseudomonas) cepacia AC1100 (33) and from a Flavobacterium sp. (34) have been purified to homogeneity. Other polychlorophenol dehalogenases were partially purified from an Arthrobacter sp. (23) or found to be membrane-associated enzymes in Rhodococcus chlorophenolicus (26,27) and Mycobacterium fortuitum (28).The dehalogenation of 2,4,6-trichlorophenol (TCP) was detected in crude extracts of Streptomyces rochei 303 (7) and Pseudomonas pickettii (12). The conversion of TCP to 2,6-dichlorohydroquinone was also observed with whole cells from Pseudomonas cepacia AC1100 (25).In this paper, we describe the purification and characterization of a TCP-dehalogenating enzyme from t...

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γ-Resorcylate Catabolic-Pathway Genes in the Soil Actinomycete Rhodococcus jostii RHA1

Kasai

Araki

Motoi

et al. 2015

Appl Environ Microbiol

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The Rhodococcus jostii RHA1 gene cluster required for ␥-resorcylate (GRA) catabolism was characterized. The cluster includes tsdA, tsdB, tsdC, tsdD, tsdR, tsdT, and tsdX, which encode GRA decarboxylase, resorcinol 4-hydroxylase, hydroxyquinol 1,2-dioxygenase, maleylacetate reductase, an IclR-type regulator, a major facilitator superfamily transporter, and a putative hydrolase, respectively. The tsdA gene conferred GRA decarboxylase activity on Escherichia coli. Purified TsdB oxidized NADH in the presence of resorcinol, suggesting that tsdB encodes a unique NADH-specific single-component resorcinol 4-hydroxylase. Mutations in either tsdA or tsdB resulted in growth deficiency on GRA. The tsdC and tsdD genes conferred hydroxyquinol 1,2-dioxygenase and maleylacetate reductase activities, respectively, on E. coli. Inactivation of tsdT significantly retarded the growth of RHA1 on GRA. The growth retardation was partially suppressed under acidic conditions, suggesting the involvement of tsdT in GRA uptake. Reverse transcription-PCR analysis revealed that the tsd genes constitute three transcriptional units, the tsdBADC and tsdTX operons and tsdR. Transcription of the tsdBADC and tsdTX operons was induced during growth on GRA. Inactivation of tsdR derepressed transcription of the tsdBADC and tsdTX operons in the absence of GRA, suggesting that tsd gene transcription is negatively regulated by the tsdR-encoded regulator. Binding of TsdR to the tsdR-tsdB and tsdT-tsdR intergenic regions was inhibited by the addition of GRA, indicating that GRA interacts with TsdR as an effector molecule.

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Characterization of the Rhodococcus sp. BPG‐8 resorcinol hydroxylase

Cited by 3 publications

References 13 publications

Targeting of proteins to the Golgi apparatus

Targeting of proteins to the Golgi apparatus

Purification and characterization of 2,4,6-trichlorophenol-4-monooxygenase, a dehalogenating enzyme from Azotobacter sp. strain GP1

γ-Resorcylate Catabolic-Pathway Genes in the Soil Actinomycete Rhodococcus jostii RHA1

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