Prdx3 protein [Mus musculus]
Protein Classification
peroxiredoxin( domain architecture ID 10122432)
peroxiredoxin, also called thioredoxin peroxidase or alkyl hydroperoxide reductase, is a thiol-specific antioxidant protein that protects cells against reactive oxygen species
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| PRX_Typ2cys | cd03015 | Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ... |
66-236 | 7.94e-117 | ||||
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure. : Pssm-ID: 239313 Cd Length: 173 Bit Score: 331.39 E-value: 7.94e-117
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| Name | Accession | Description | Interval | E-value | ||||
| PRX_Typ2cys | cd03015 | Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ... |
66-236 | 7.94e-117 | ||||
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure. Pssm-ID: 239313 Cd Length: 173 Bit Score: 331.39 E-value: 7.94e-117
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| AhpC | COG0450 | Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms]; |
63-254 | 4.09e-107 | ||||
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms]; Pssm-ID: 440219 Cd Length: 196 Bit Score: 307.77 E-value: 4.09e-107
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| PTZ00253 | PTZ00253 | tryparedoxin peroxidase; Provisional |
70-252 | 1.06e-98 | ||||
tryparedoxin peroxidase; Provisional Pssm-ID: 140280 Cd Length: 199 Bit Score: 286.80 E-value: 1.06e-98
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| AhpC | TIGR03137 | peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ... |
63-244 | 5.27e-68 | ||||
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions] Pssm-ID: 211789 Cd Length: 187 Bit Score: 208.41 E-value: 5.27e-68
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| peroxi_PrxU | NF040737 | thioredoxin-dependent peroxiredoxin; |
66-245 | 2.41e-57 | ||||
thioredoxin-dependent peroxiredoxin; Pssm-ID: 468701 Cd Length: 233 Bit Score: 182.55 E-value: 2.41e-57
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| AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
66-198 | 3.09e-48 | ||||
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA). Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 155.46 E-value: 3.09e-48
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| Name | Accession | Description | Interval | E-value | ||||
| PRX_Typ2cys | cd03015 | Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ... |
66-236 | 7.94e-117 | ||||
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure. Pssm-ID: 239313 Cd Length: 173 Bit Score: 331.39 E-value: 7.94e-117
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| AhpC | COG0450 | Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms]; |
63-254 | 4.09e-107 | ||||
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms]; Pssm-ID: 440219 Cd Length: 196 Bit Score: 307.77 E-value: 4.09e-107
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| PTZ00253 | PTZ00253 | tryparedoxin peroxidase; Provisional |
70-252 | 1.06e-98 | ||||
tryparedoxin peroxidase; Provisional Pssm-ID: 140280 Cd Length: 199 Bit Score: 286.80 E-value: 1.06e-98
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| AhpC | TIGR03137 | peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ... |
63-244 | 5.27e-68 | ||||
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions] Pssm-ID: 211789 Cd Length: 187 Bit Score: 208.41 E-value: 5.27e-68
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| PTZ00137 | PTZ00137 | 2-Cys peroxiredoxin; Provisional |
48-254 | 2.77e-60 | ||||
2-Cys peroxiredoxin; Provisional Pssm-ID: 173427 Cd Length: 261 Bit Score: 191.31 E-value: 2.77e-60
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| PRK15000 | PRK15000 | peroxiredoxin C; |
66-252 | 9.59e-60 | ||||
peroxiredoxin C; Pssm-ID: 184962 Cd Length: 200 Bit Score: 187.96 E-value: 9.59e-60
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| peroxi_PrxU | NF040737 | thioredoxin-dependent peroxiredoxin; |
66-245 | 2.41e-57 | ||||
thioredoxin-dependent peroxiredoxin; Pssm-ID: 468701 Cd Length: 233 Bit Score: 182.55 E-value: 2.41e-57
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| PRX_family | cd02971 | Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ... |
70-214 | 6.55e-57 | ||||
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis. Pssm-ID: 239269 [Multi-domain] Cd Length: 140 Bit Score: 178.13 E-value: 6.55e-57
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| PRK10382 | PRK10382 | alkyl hydroperoxide reductase subunit C; Provisional |
67-244 | 6.24e-50 | ||||
alkyl hydroperoxide reductase subunit C; Provisional Pssm-ID: 182423 Cd Length: 187 Bit Score: 162.08 E-value: 6.24e-50
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| AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
66-198 | 3.09e-48 | ||||
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA). Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 155.46 E-value: 3.09e-48
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| PRK13190 | PRK13190 | putative peroxiredoxin; Provisional |
68-255 | 1.21e-43 | ||||
putative peroxiredoxin; Provisional Pssm-ID: 106159 Cd Length: 202 Bit Score: 146.54 E-value: 1.21e-43
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| PRK13189 | PRK13189 | peroxiredoxin; Provisional |
70-250 | 5.05e-42 | ||||
peroxiredoxin; Provisional Pssm-ID: 237297 Cd Length: 222 Bit Score: 142.81 E-value: 5.05e-42
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| PRX_1cys | cd03016 | Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ... |
87-250 | 1.43e-39 | ||||
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins. Pssm-ID: 239314 Cd Length: 203 Bit Score: 136.13 E-value: 1.43e-39
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| PRK13191 | PRK13191 | putative peroxiredoxin; Provisional |
89-257 | 9.09e-36 | ||||
putative peroxiredoxin; Provisional Pssm-ID: 183885 Cd Length: 215 Bit Score: 126.50 E-value: 9.09e-36
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| PRX_AhpE_like | cd03018 | Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ... |
70-209 | 9.14e-33 | ||||
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers. Pssm-ID: 239316 [Multi-domain] Cd Length: 149 Bit Score: 116.60 E-value: 9.14e-33
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| PRK13599 | PRK13599 | peroxiredoxin; |
89-242 | 2.92e-29 | ||||
peroxiredoxin; Pssm-ID: 106544 [Multi-domain] Cd Length: 215 Bit Score: 109.80 E-value: 2.92e-29
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| Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
70-215 | 7.41e-29 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 106.10 E-value: 7.41e-29
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| PRX_BCP | cd03017 | Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ... |
68-215 | 8.53e-29 | ||||
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth. Pssm-ID: 239315 Cd Length: 140 Bit Score: 106.09 E-value: 8.53e-29
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| PRX_Atyp2cys | cd03014 | Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ... |
65-198 | 1.01e-18 | ||||
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs. Pssm-ID: 239312 [Multi-domain] Cd Length: 143 Bit Score: 79.94 E-value: 1.01e-18
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| Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
65-205 | 1.64e-15 | ||||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 71.63 E-value: 1.64e-15
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| tpx | PRK00522 | thiol peroxidase; |
64-198 | 1.10e-13 | ||||
thiol peroxidase; Pssm-ID: 179055 Cd Length: 167 Bit Score: 66.85 E-value: 1.10e-13
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| 1-cysPrx_C | pfam10417 | C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ... |
219-254 | 2.23e-11 | ||||
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerization of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme. The domain is associated with family AhpC-TSA, pfam00578, which carries the catalytic cysteine. Pssm-ID: 431271 Cd Length: 40 Bit Score: 57.21 E-value: 2.23e-11
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| bcp | PRK09437 | thioredoxin-dependent thiol peroxidase; Reviewed |
80-199 | 5.27e-09 | ||||
thioredoxin-dependent thiol peroxidase; Reviewed Pssm-ID: 181857 Cd Length: 154 Bit Score: 53.79 E-value: 5.27e-09
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| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
65-198 | 5.52e-08 | ||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 50.46 E-value: 5.52e-08
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| TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
82-198 | 5.14e-06 | ||||
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases. Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 44.53 E-value: 5.14e-06
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| PRX5_like | cd03013 | Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ... |
79-201 | 1.90e-04 | ||||
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs. Pssm-ID: 239311 [Multi-domain] Cd Length: 155 Bit Score: 40.62 E-value: 1.90e-04
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| Thioredoxin_8 | pfam13905 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
93-196 | 2.50e-04 | ||||
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Pssm-ID: 464033 [Multi-domain] Cd Length: 95 Bit Score: 39.21 E-value: 2.50e-04
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| Sco1 | COG1999 | Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
84-219 | 3.06e-04 | ||||
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441602 Cd Length: 156 Bit Score: 40.27 E-value: 3.06e-04
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| SCO | cd02968 | SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ... |
84-196 | 8.79e-04 | ||||
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II. Pssm-ID: 239266 Cd Length: 142 Bit Score: 38.74 E-value: 8.79e-04
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