Crystal Structure of Lactoperoxidase at 2.4 Å Resolution

Singh, Amit Kumar; Singh, Nagendra; Sharma, Sujata; Singh, Sanjay; Kaur, Punit; Bhushan, A.; Srinivasan, A.; Singh, T.P.

doi:10.1016/j.jmb.2007.12.012

Cited by 104 publications

(113 citation statements)

References 37 publications

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“…This matches with five N-glycans in mature homodimeric MPO and pro-MPO produced in CHO cell lines (21). Monomeric bovine lactoperoxidase has four N-glycosylation sites (38). Furthermore, the peroxidase domain of hsPxd01 was shown to be stabilized by seven confirmed disulfide bridges, including the propeptide region.…”

Section: Journal Of Biological Chemistry 10885supporting

confidence: 60%

Multidomain Human Peroxidasin 1 Is a Highly Glycosylated and Stable Homotrimeric High Spin Ferric Peroxidase

Soudi

Paumann-Page

Delporte

et al. 2015

Journal of Biological Chemistry

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Background: Human peroxidasin 1 (hsPxd01) mediates the formation of sulfilimine cross-links within the collagen IV scaffold of basement membranes. Results: Overexpressed hsPxd01 contains covalently linked heme catalytically active for production of hypobromous acid. Conclusion: hsPxd01 has peroxidase-like active site structure but restricted substrate accessibility. Significance: Architecture of hsPxd01 facilitates product release and its interactions with the physiological substrate collagen IV.

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Section: Journal Of Biological Chemistry 10885supporting

confidence: 60%

Multidomain Human Peroxidasin 1 Is a Highly Glycosylated and Stable Homotrimeric High Spin Ferric Peroxidase

Soudi

Paumann-Page

Delporte

et al. 2015

Journal of Biological Chemistry

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“…1B. This partial sequence alignment with the classical peroxidases demonstrates that both DUOX homologs lack the catalytic distal histidine residue (Ser 108 , hDUOX1; and Tyr 105 , CeDUOX1) and the aspartate residue that in MPO and LPO covalently binds to the heme co-factor through an ester linkage (Leu 107 , hDUOX1; and Ala 104 , CeDUOX1) (25,26). hDUOX1 lacks additional critical peroxidase residues: the glutamate that forms the second covalent bond to the heme (Arg 241 ) and the proximal histidine residue (Ser 331 ).…”

Section: Design and Expression Of Soluble Duox1mentioning

confidence: 85%

Caenorhabditis elegans and Human Dual Oxidase 1 (DUOX1) “Peroxidase” Domains

Meitzler

Montellano

2009

Journal of Biological Chemistry

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The seven members of the NOX/DUOX family are responsible for generation of the superoxide and H 2 O 2 required for a variety of host defense and cell signaling functions in nonphagocytic cells. Two members, the dual oxidase isozymes DUOX1 and DUOX2, share a structurally unique feature: an N-terminal peroxidase-like domain. Despite sequence similarity to the mammalian peroxidases, the absence of key active site residues makes their binding of heme and their catalytic function uncertain. To explore this domain we have expressed in a baculovirus system and purified the Caenorhabditis elegans (CeDUOX1 1-589 ) and human (hDUOX1 1-593 ) DUOX1 "peroxidase" domains. Evaluation of these proteins demonstrated that the isolated hDUOX1 1-593 does not bind heme and has no intrinsic peroxidase activity. In contrast, CeDUOX1 1-589 binds heme covalently, exhibits a modest peroxidase activity, but does not oxidize bromide ion. Surprisingly, the heme appears to have two covalent links to the protein despite the absence of a second conserved carboxyl group in the active site. Although the N-terminal dual oxidase motif has been proposed to directly convert superoxide to H 2 O 2 , neither DUOX1 domain demonstrated significant superoxide dismutase activity. These results strengthen the in vivo conclusion that the CeDUOX1 protein supports controlled peroxidative polymerization of tyrosine residues and indicate that the hDUOX1 protein either has a unique function or must interact with other protein factors to express its catalytic activity.

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“…Animal heme peroxidases are known to require a heme prosthetic group. This heme group is covalently attached to aspartate and glutamate residues in LPO (34) and to an additional methionine in MPO (31). The heme is also hydrogen bonded to a proximal histidine which interacts with an essential asparagine (35,36).…”

Section: Resultsmentioning

confidence: 99%

Heterologous Expression and Characterization of the Manganese-Oxidizing Protein from Erythrobacter sp. Strain SD21

Nakama

Medina

Lien

et al. 2014

Appl Environ Microbiol

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The manganese (Mn)-oxidizing protein (MopA) from Erythrobacter sp. strain SD21 is part of a unique enzymatic family that is capable of oxidizing soluble Mn(II). This enzyme contains two domains, an animal heme peroxidase domain, which contains the catalytic site, followed by a C-terminal calcium binding domain. Different from the bacterial Mn-oxidizing multicopper oxidase enzymes, little is known about MopA. To gain a better understanding of MopA and its role in Mn(II) oxidation, the 238-kDa fulllength protein and a 105-kDa truncated protein containing only the animal heme peroxidase domain were cloned and heterologously expressed in Escherichia coli. Despite having sequence similarity to a peroxidase, hydrogen peroxide did not stimulate activity, nor was activity significantly decreased in the presence of catalase. Both pyrroloquinoline quinone (PQQ) and hemin increased Mn-oxidizing activity, and calcium was required. The K m for Mn(II) of the full-length protein in cell extract was similar to that of the natively expressed protein, but the K m value for the truncated protein in cell extract was approximately 6-fold higher than that of the full-length protein, suggesting that the calcium binding domain may aid in binding Mn(II). Characterization of the heterologously expressed MopA has provided additional insight into the mechanism of bacterial Mn(II) oxidation, which will aid in understanding the role of MopA and Mn oxidation in bioremediation and biogeochemical cycling.

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Crystal Structure of Lactoperoxidase at 2.4 Å Resolution

Cited by 104 publications

References 37 publications

Multidomain Human Peroxidasin 1 Is a Highly Glycosylated and Stable Homotrimeric High Spin Ferric Peroxidase

Multidomain Human Peroxidasin 1 Is a Highly Glycosylated and Stable Homotrimeric High Spin Ferric Peroxidase

Caenorhabditis elegans and Human Dual Oxidase 1 (DUOX1) “Peroxidase” Domains

Heterologous Expression and Characterization of the Manganese-Oxidizing Protein from Erythrobacter sp. Strain SD21

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