KatB, a cyanobacterial Mn-catalase with unique active site configuration: Implications for enzyme function

Bihani, Subhash C.; Chakravarty, Dhiman; Ballal, Anand

doi:10.1016/j.freeradbiomed.2016.01.022

Cited by 22 publications

(17 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, the catalase is supposed to be a homo-hexamer enzyme like manganese catalases from Lactobacillus plantarum [19], Thermus thermophiles [20], Thermus sp. YS 8-13 [21], and Anabaena PCC7120 [24]. Kinetic analysis of GWC shows a K m value of 67.26 mM and a k cat value of 2.9 × 10 4 s −1 subunit −1 toward H 2 O 2 .…”

Section: Discussionmentioning

confidence: 98%

“…Unlike most manganese catalases, GWC has no C-terminal tail revealed by SWISS-MODEL. Hydrogen bonds and salt bridges are the main forces of its homo-hexamer assembly, and a loss of the C-terminal tail contributes to smaller number of hydrogen bonds and salt bridges [24]. Moreover, the Ca 2+ binding site in the C-terminal tail may stabilize the homo-hexamer structure [24].…”

Section: Discussionmentioning

confidence: 99%

“…Hydrogen bonds and salt bridges are the main forces of its homo-hexamer assembly, and a loss of the C-terminal tail contributes to smaller number of hydrogen bonds and salt bridges [24]. Moreover, the Ca 2+ binding site in the C-terminal tail may stabilize the homo-hexamer structure [24]. Therefore, the homo-hexamer structure of GWC may not be as stable as that of other manganese catalases from Thermus sp.…”

Section: Discussionmentioning

confidence: 99%

“…Several manganese catalases have been reported to have a homo-hexamer structure such as LPC, TTC, and KatB [24]. In this study, we first determine the subunit molecular mass from SDS-PAGE.…”

Section: Manganese Catalase Identificationmentioning

confidence: 99%

“…They are Lactobacillus plantarum (LPC) [19], Thermus thermophiles (TTC) [20], Thermus sp. YS 8-13 [21], Thermoleophilum album [22], Pyrobaculum caldifontis VA1 [23], Anabaena PCC7120 (KatB) [24], and Thermomicrobium roseum [25]. Purification of the Mn-containing catalases is difficult because the expression level of wild-type catalase is very low.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

A New Homo-Hexamer Mn-Containing Catalase from Geobacillus sp. WCH70

Wang

et al. 2017

Catalysts

View full text Add to dashboard Cite

Abstract:Catalase is an effective biocatalyst to degrade hydrogen peroxide to water and oxygen that can serve in textile effluent treatment to remove residual H 2 O 2 . Thermostable catalases are needed to withstand both the high temperature and pH of textile wastewater. We have cloned the Mn-containing catalase gene ACS24898.1 from Geobacillus sp. WCH70, which originated from thermophilic organisms, and expressed it in Escherichia coli in activated form. The recombinant protein has been purified to homogeneity and identified to be a new homo-hexamer Mn-containing catalase. The native molecular mass of the catalase has been measured to be 138 kDa by size-exclusion chromatography. The new enzyme has optimum catalyzed activity at pH 9.0 and a temperature of 75 • C. It is thermostable up to 70 • C for 8 h incubation and maintains 80% and 50% activity, respectively, at 80 • C after 5 h and 90 • C after 1 h. At 75 • C and pH 9.0, the K m is 67.26 mM for substrate H 2 O 2 and the rate of reaction at H 2 O 2 saturation, V max , is 75,300 U/mg. The thermophilic and alkaline preferred properties of this new Mn-catalase are valuable features in textile wastewater treatment.

show abstract

Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Manganese Catalase Identificationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A New Homo-Hexamer Mn-Containing Catalase from Geobacillus sp. WCH70

Wang

et al. 2017

Catalysts

View full text Add to dashboard Cite

show abstract

Assembly of Dimanganese and Heterometallic Manganese Proteins

Berggren

Lundin

Sjöberg

2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

Manganese is an essential trace element in all domains of life, and manganese‐dependent enzymes catalyze a wide range of reactions including hydrolysis, phosphorylation, water oxidation, nucleotide reduction, and protection against oxidative stress. Dinuclear manganese‐containing cofactors are both homonuclear and heteronuclear centers. Due to its rich redox chemistry, manganese is found in a number of redox‐active enzymes, where the oxidation state of the metal ion ranges from Mn II to Mn IV . Non‐redox‐active metal sites are found in, for example, sweet potato purple acid phosphatase (Mn II Fe III ), concanavalin A (Mn II Ca II ), arginase (Mn II 2 ), and prolidase (Mn II 2 ). Proteins with redox‐active Mn‐containing dinuclear centers generally belong to the ferritin‐like superfamily. Whereas most members of the superfamily have an Fe 2 center, Mn‐containing metal sites are found in Mn catalase (Mn 2 ), some RNR β subunits (subclasses Ib and Id have Mn 2 , and subclass Ic has MnFe), and R2lox (MnFe). In addition, a member of DNA‐binding protein from starved cells ( Dps ) can form an MnFe center. No manganese chaperones are known and Mn‐dependent enzymes plausibly acquire their metals directly from the intracellular pool of Mn 2+ , which is balanced via different import and efflux transporter systems: Mn catalase catalyzes the disproportionation of the reactive species hydrogen peroxide by alternating between Mn III 2 and Mn II 2 in two consecutive reactions, detoxifying two hydrogen peroxide molecules to oxygen and water. RNR subclass Ib β subunit has an oxidized metal center and a tyrosyl radical. It initially binds Mn 2+ and forms a complex with a specific flavodoxin‐like protein that oxidizes the metal center to a transient Mn IV/III species, which converts to the active Mn III 2 ‐Tyr • cofactor. RNR subclass Ic β subunit has an Mn IV Fe III cofactor. It is formed by O 2 oxidation of a Mn II Fe II center, and the initial transient Mn IV Fe IV center is reduced to the active cofactor via an external electron transfer pathway. RNR subclass Id β subunit is suggested to contain an oxidized Mn 2 center formed in the absence of a flavodoxin‐like maturase and lacks the tyrosyl radical. R2‐like ligand‐binding oxidase (R2lox) has an Mn III Fe III cofactor that is generated from Mn II Fe II by O 2 oxidation. It is assumed that an Mn IV Fe IV intermediate generates a valine–tyrosine cross‐link adjacent to the metal site. Despite the apparent simplicity of manganese cofactor assembly, nature has developed a number of different methods to control the metalation of manganese proteins and activate the relatively redox‐inert Mn II ion.

show abstract

Theoretical study of the mechanism of the manganese catalase KatB

Yang

Mao

et al. 2018

J Biol Inorg Chem

View full text Add to dashboard Cite

KatB, a cyanobacterial Mn-catalase with unique active site configuration: Implications for enzyme function

Cited by 22 publications

References 61 publications

A New Homo-Hexamer Mn-Containing Catalase from Geobacillus sp. WCH70

A New Homo-Hexamer Mn-Containing Catalase from Geobacillus sp. WCH70

Assembly of Dimanganese and Heterometallic Manganese Proteins

Theoretical study of the mechanism of the manganese catalase KatB

Contact Info

Product

Resources

About