Reinvestigation of metal ion specificity for quinone cofactor biogenesis in bacterial copper amine oxidase

Okajima, T.; Kishishita, S.; Chiu, Y.C.; Murakawa, T.; Kim, M.; Yamaguchi, H.; Hirota, S.; Kuroda, S.; Tanizawa, K.; Biochemistry 44, 12041-12048 (2005)

 show all sequences of 1.4.3.21

Data extracted from this reference:

Crystallization (Commentary)
Crystallization Organism
holenzyme, in which topaquinone is generated by incubation with Co2+ or Ni2+ and apoenzyme are crystallized by microdialysis method Arthrobacter globiformis
KM Value [mM]
KM Value [mM] KM Value Maximum [mM] Substrate Commentary Organism Structure
0.0025
-
 2-Phenylethylamine pH 6.8, 30°C, Co-activated enzyme; pH 6.8, 30°C, Cu-activated enzyme Arthrobacter globiformis
0.0034
-
 2-Phenylethylamine pH 6.8, 30°C, Ni-activated enzyme Arthrobacter globiformis
Metals/Ions
Metals/Ions Commentary Organism Structure
Co2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
Cu2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
Ni2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
Zn2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently Arthrobacter globiformis
Organism
Organism Primary Accession No. (UniProt) Commentary Textmining
Arthrobacter globiformis P46881
-
-
Purification (Commentary)
Commentary Organism
recombinant enzyme expressed in Escherichia coli Arthrobacter globiformis
Substrates and Products (Substrate)
Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility
2-phenylethylamine + H2O + O2
-
 671976 Arthrobacter globiformis 2-phenylethanal + NH3 + H2O2
-
-
-
 ?
Turnover Number [1/s]
Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Commentary Organism Structure
0.63
-
 2-Phenylethylamine pH 6.8, 30°C, Ni-activated enzyme Arthrobacter globiformis
0.92
-
 2-Phenylethylamine pH 6.8, 30°C, Co-activated enzyme Arthrobacter globiformis
75.7
-
 2-Phenylethylamine pH 6.8, 30°C, Cu-activated enzyme Arthrobacter globiformis
Crystallization (Commentary) (protein specific)
Crystallization Organism
holenzyme, in which topaquinone is generated by incubation with Co2+ or Ni2+ and apoenzyme are crystallized by microdialysis method Arthrobacter globiformis
KM Value [mM] (protein specific)
KM Value [mM] KM Value Maximum [mM] Substrate Commentary Organism Structure
0.0025
-
 2-Phenylethylamine pH 6.8, 30°C, Co-activated enzyme; pH 6.8, 30°C, Cu-activated enzyme Arthrobacter globiformis
0.0034
-
 2-Phenylethylamine pH 6.8, 30°C, Ni-activated enzyme Arthrobacter globiformis
Metals/Ions (protein specific)
Metals/Ions Commentary Organism Structure
Co2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
Cu2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
Ni2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
Zn2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently Arthrobacter globiformis
Purification (Commentary) (protein specific)
Commentary Organism
recombinant enzyme expressed in Escherichia coli Arthrobacter globiformis
Substrates and Products (Substrate) (protein specific)
Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility
2-phenylethylamine + H2O + O2
-
 671976 Arthrobacter globiformis 2-phenylethanal + NH3 + H2O2
-
-
-
 ?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Commentary Organism Structure
0.63
-
 2-Phenylethylamine pH 6.8, 30°C, Ni-activated enzyme Arthrobacter globiformis
0.92
-
 2-Phenylethylamine pH 6.8, 30°C, Co-activated enzyme Arthrobacter globiformis
75.7
-
 2-Phenylethylamine pH 6.8, 30°C, Cu-activated enzyme Arthrobacter globiformis

See also following references to EC number 1.4.3.21 (sorted by year of publication):
No.1st authorPub
Med		titleorganimsjournalvolumepagesyearActivating CompoundApplicationCloned(Commentary)Crystallization (Commentary)EngineeringGeneral StabilityInhibitorsKM Value [mM]LocalizationMetals/IonsMolecular Weight [Da]Natural Substrates/ Products (Substrates)Organic Solvent StabilityOrganismOxidation StabilityPosttranslational ModificationPurification (Commentary)ReactionRenatured (Commentary)Source TissueSpecific Activity [micromol/min/mg]Storage StabilitySubstrates and Products (Substrate)SubunitsTemperature Optimum [°C]Temperature Range [°C]Temperature Stability [°C]Turnover Number [1/s]pH OptimumpH RangepH StabilityCofactorKi Value [mM]pI ValueIC50 ValueActivating Compound (protein specific)Application (protein specific)Cloned(Commentary) (protein specific)Cofactor (protein specific)Crystallization (Commentary) (protein specific)Engineering (protein specific)General Stability (protein specific)IC50 Value (protein specific)Inhibitors (protein specific)Ki Value [mM] (protein specific)KM Value [mM] (protein specific)Localization (protein specific)Metals/Ions (protein specific)Molecular Weight [Da] (protein specific)Natural Substrates/ Products (Substrates) (protein specific)Organic Solvent Stability (protein specific)Oxidation Stability (protein specific)Posttranslational Modification (protein specific)Purification (Commentary) (protein specific)Renatured (Commentary) (protein specific)Source Tissue (protein specific)Specific Activity [micromol/min/mg] (protein specific)Storage Stability (protein specific)Substrates and Products (Substrate) (protein specific)Subunits (protein specific)Temperature Optimum [°C] (protein specific)Temperature Range [°C] (protein specific)Temperature Stability [°C] (protein specific)Turnover Number [1/s] (protein specific)pH Optimum (protein specific)pH Range (protein specific)pH Stability (protein specific)pI Value (protein specific)ExpressionGeneral InformationGeneral Information (protein specific)Expression (protein specific)KCat/KM [mM/s]KCat/KM [mM/s] (protein specific)
710834StevanatoPreliminary kinetic characteri ...Rattus norvegicusAmino Acids40713-7202010-------121---4-----2--1------1---------------121-------2--1------1--------
711430LiangA conformationally constrained ...Homo sapiensBioorg. Med. Chem. Lett.206721-67242010--1---1-11-1-1--------31-------1-----11----1--11-1--------31--------------
711738HaiderSynthesis of ortho-functionali ...Homo sapiensChem. Pharm. Bull.58964-9702010------12--1---1--------------1-----1-------112---1----------------1---------
712709NurminenSynthesis, in vitro activity, ...Homo sapiensJ. Med. Chem.536301-63152010-11---54--1-1-2--------2-1---1-------11-----54---1-1--------2-1---1---------
701561NunesSemicarbazide-sensitive amine ...Homo sapiensActa Diabetol.46135-1402009---------1-2-1-----10--3-1---1--1------1--------1-2-----10--3-1---1----11---
701612BourSemicarbazide-sensitive amine ...Mus musculusAm. J. Pathol.1741075-10832009----1---1----4-----3--------------------1-----1--------3------------1221--
703130KaitaniemiThe unique substrate specifici ...Homo sapiensCell. Mol. Life Sci.662743-27572009--1-1-5821-8-4-----14--121--------3----2--1--73932-8-----16--122--------------
705350Iffiu-SolteszInfluence of prolonged fasting ...Rattus norvegicusJ. Physiol. Biochem.6511-2320091-----2-1----4-----1--2------------1-------2--1--------1--2---------------
705496VavilovaMonoamine oxidase and semicarb ...Homo sapiensMed. Sci. Monit.15BR289-BR2922009------1----1-1-----1--1--------------------1-----1-----1--1----------11---
712188MarteliusInhibition of semicarbazide-se ...Rattus norvegicusInt. J. Immunopathol. Pharmacol.21911-9202009------1-21---3-----5--11-------------------1--21-------5--11---------11---
684124DaiSynthetic liver X receptor ago ...Mus musculusActa Biochim. Biophys. Sin. (Shanghai)40261-2682008-----------1-1--------2--------------------------1--------2---------------
686264DunkelSemicarbazide-sensitive amine ...Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicusCurr. Med. Chem.151827-18392008------45------6-----5--26-----------45-------4545-----------5--26---------------
686850LinAntioxidant, anti-semicarbazid ...Bos taurusFood Chem. Toxicol.462485-24922008------1------1-----1--1---------1-1-------111----------1--1---------------
687077FracassiniEndogenous substrates of the s ...Rattus norvegicusInflamm. Res.57S53-S542008------1------1-----1--1--------------------1-----------1--1---------------
687307LangleyEnantiomer-specific binding of ...Arthrobacter globiformisJ. Am. Chem. Soc.1308069-80782008---1--1------3--------1----------------1---1--------------1---------------
687459LeePurification and characterizat ...Mycobacterium sp., Mycobacterium sp. JC1J. Biochem.144107-1142008------62-12--3--1--152-32----1--1------1----6-2-12----1-152-32----1---------
688002WiwanitkitSynergistic interaction betwee ...Homo sapiensJ. Diabetes Complicat.22413-4192008-----------1-1--------1--------------------------1--------1---------------
688100AnHydrogen peroxide generated by ...Vicia fabaJ. Exp. Bot.59815-8252008-------------3-----1-----------------------------------1------------------
688553SibonAssociation between semicarbaz ...Rattus norvegicusJ. Neurosurg.108558-5662008-------------1--------1-----------------------------------1---------------
688603ORourkeAnti-inflammatory effects of L ...Homo sapiens, Mus musculus, Rattus norvegicusJ. Pharmacol. Exp. Ther.324867-8752008------3------3-----3--3-----------4-------43-----------3--3---------------
689200JiangThe contribution of cerebral v ...Homo sapiensNeuropathol. Appl. Neurobiol.34194-2042008-------------1-----1-----------------------------------1------------------
689377CarpeneLimitation of adipose tissue e ...Rattus norvegicusPharmacol. Res.57426-4342008------2------4-----3--1--------------------2-----------3--1---------------
701483PirratStructure of a xenon derivativ ...Escherichia coliActa Crystallogr. Sect. F641105-11092008---1-----1---2--------11-------1------11-------1----------11--------------
701487AtkinCloning, expression, purificat ...Aspergillus nigerActa Crystallogr. Sect. F64182-1852008--113-2------1--1-----11-------1-----1113--2---------1----11--------------
701490LangleyComplexes of the copper-contai ...Arthrobacter globiformisActa Crystallogr. Sect. F64577-5832008---1--2--1---3-----------------1------11---2---1--------------------------
703506PeterCopper distributed by Atx1 is ...no activity in Saccharomyces cerevisiae, Schizosaccharomyces pombe, Schizosaccharomyces pombe FY435Eukaryot. Cell71781-179420082-1-5----1-1-5--------211---1--1---2-11-5------1-1--------211---1----11---
705128AtkinThe structure of monoamine oxi ...Aspergillus nigerJ. Mol. Biol.3841218-12312008--112------1-1-11-----11-------1-----1112--------1--11----11--------------
684285GokturkMacrovascular changes in mice ...Homo sapiensAm. J. Hypertens.20743-7502007--1--------1-1--------2--------------1-----------1--------2---------------
684685Di PaoloN-alkanamines as substrates to ...Bos taurusArch. Biochem. Biophys.46550-602007-------------3--1--1--6------------------------------1-1--6---------------
685663WangDPPH radical scavenging and se ...Homo sapiens, Mus musculusBiosci. Biotechnol. Biochem.711873-18782007------2------2-----2--2--------------------2-----------2--2---------------
686052YraolaUnderstanding the mechanism of ...Homo sapiens, Mus musculus, Rattus norvegicusChem. Biol. Drug Des.69423-4282007-3-----62----3-----2--6-------------3--------62--------2--6---------------
686502RoessnerDecreased serum activity of se ...Homo sapiensEur. J. Clin. Pharmacol.63425-4292007-------------1-----1--1--------------------------------1--1---------------
687276MooreTrapping of a dopaquinone inte ...Arthrobacter globiformisJ. Am. Chem. Soc.12911524-115342007---12----1---3--1-----1--------1------112------1-----1----1---------------
687449Hernandez-GuillamonSodium bicarbonate enhances me ...Homo sapiensJ. Biochem.142571-5762007--------21---1-----2--1-----------------------21-------2--1---------------
688255LeonettiSolid-phase synthesis and insi ...Homo sapiensJ. Med. Chem.504909-49162007------1------1-----2--1--------------------1-----------2--1---------------
688482OlivieriL-lysine as a recognition mole ...Bos taurusJ. Neural Transm.114747-7492007------1----1-1-----1--2---------1----------11----1-----1--2---------------
688483O'SullivanHydrogen peroxide derived from ...Bos taurusJ. Neural Transm.114751-7562007------1------2-----1--1--------------------1-----------1--1---------------
688484YabanogluInteraction of rat lung SSAO w ...Rattus norvegicusJ. Neural Transm.114769-7732007------4---1--1--1--11-11--------8----------48---1----1-11-11--------------
688487BourSemicarbazide-sensitive amine ...Mus musculusJ. Neural Transm.114829-8332007-------------4-----2--1--------------------------------2--1---------------
688488NemcsikAlteration of serum semicarbaz ...Homo sapiensJ. Neural Transm.114841-8432007-------------1-----1--1--------------------------------1--1---------------
688489SolteszStudies on the insulinomimetic ...Rattus norvegicusJ. Neural Transm.114851-8552007-------------4-----1--1--------------------------------1--1---------------
688490UnzetaSemicarbazide-sensitive amine ...Homo sapiensJ. Neural Transm.114857-8622007-----------1-1-----2--1--------------------------1-----2--1---------------
688491VidrioHypotensive effect of hydroxyl ...Rattus norvegicusJ. Neural Transm.114863-8652007------1------1--------1--------------------1--------------1---------------
688757TakahashiAbsence of tissue-bound semica ...no activity in Cyprinus carpioLife Sci.801094-10992007-------------1------------------------------------------------------------
689375CarpeneReduction of fat deposition by ...Rattus norvegicusPharmacol. Res.56522-5302007------1------2-----1--2--------------------1-----------1--2---------------
689376PrevotProlonged treatment with amino ...Rattus norvegicusPharmacol. Res.5670-792007------1------1-----1--1--------------------1-----------1--1---------------
671747MurakawaQuantum mechanical hydrogen tu ...Arthrobacter globiformisBiochem. Biophys. Res. Commun.342414-4232006-------------2--------1-----------------------------------1---------------
672133DuBoisRole of a strictly conserved a ...Ogataea angustaBiochemistry453178-31882006----2--------4--------3----3------------2-----------------3----3----------
672146ChiuKinetic and structural studies ...Arthrobacter globiformisBiochemistry454105-41202006----1--2-----4--------1----2-1----------1----2------------1----2-1--------
672152TakahashiRelationship of stopped flow t ...Ogataea angustaBiochemistry454683-46942006---------2---5--------1------------------------2----------1---------------
672492OchiaiSubstrate selectivity of monoa ...Rattus norvegicusBiol. Pharm. Bull.292362-23662006--1---2------1------9-5--------------1-----2------------9-5---------------
671976OkajimaReinvestigation of metal ion s ...Arthrobacter globiformisBiochemistry4412041-120482005---1---2-4---4--1-----1----3-----------1-----2-4-----1----1----3----------
675286BertiniAlkylamino derivatives of 4-am ...Ogataea angusta, Pisum sativum, Sus scrofaJ. Med. Chem.48664-6702005------472-1---6-----2--6-----------37-------3747-2-1-------2--6---------------
676364LonguMechanism-based inactivators o ...Lathyrus sativus, Lens culinaris, Onobrychis viciifolia, Pisum sativumPhytochemistry661751-17582005------383-4---4-5---2--371---4---56-----5----3863-4----5--2--371---4----------
655782KishishitaRole of copper ion in bacteria ...Arthrobacter globiformisJ. Am. Chem. Soc.1251041-10552003---1---6-3---3--1-----1----6-----------1-----6-3-----1----1----6----------
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654616MillsMechanistic comparison of the ...Ogataea angustaBiochemistry4110577-105842002-------1-2---4--------1----2-----------------1-2----------1----2----------
655781Lee3-Pyrrolines are mechanism-bas ...Bos taurusJ. Am. Chem. Soc.12412135-121432002------9--1---1-----2--1--------1------1----9---1-------2--1---------------
391960Mills-Evidence against reduction of ...Ogataea angusta, Ogataea angusta 1A2VJ. Am. Chem. Soc.1229897-99042000--1----2-1---2--113--6-2----2---------1-------2-1-----1--6-2----2----------
391956LiCopper amine oxidase from Hans ...Ogataea angusta 1A2V, Ogataea angustaStructure6293-3071998---13----1----6---13----1----------------13------1-----------1---------------
391949CaiCopper amine oxidase: heterolo ...Ogataea angusta 1A2V, Ogataea angustaBiochemistry337647-76531994--1----311---5--1---1-3--------1-----11------311-----1--1-3---------------
391937HysmithPurification of benzylamine ox ...Sus scrofaBiochem. Cell Biol.66821-8291988------51-----2--1--21-21-------------------5-1-------1-21-21--------------
391914FalkHeterogeneity of pig plasma am ...Sus scrofaBiochemistry223746-37511983------11-11--1-11--11-21---1---1------1----1-1-11---11-11-21---1----------
391932BarkerProperties of cupric ions in b ...Sus scrofaBiochem. J.177289-3021979------3--11--3-----2--11--------5----------35--11------2--11--------------
391910Carper-Pig liver monoamine oxidase I: ...Sus scrofaBiochim. Biophys. Acta334287-2961974---1--52-41--1-----11-2111--11---------1---5-2-41------11-2111--11--------
391915LindströmEffect of azide on some spectr ...Sus scrofaEur. J. Biochem.48237-2431974------4--1---1-----1--1--------11-----1----41--1-------1--1---------------
391916LindströmKinetics of the interaction be ...Sus scrofaEur. J. Biochem.42177-1821974------2------1-----1--1--------1------1----2-----------1--1---------------
391908YamadaMonoamine oxidase II. Copper, ...Bos taurusJ. Biol. Chem.2373077-30821962------61-1---1--1--1--2---------1----------611-1-----1-1--2---------------