ライフサイエンスコーパス: metalloenzyme

1 xist in an experimentally studied artificial metalloenzyme.

2 is catalyzed by nitrogenase, a two-component metalloenzyme.

3 which is inconsistent with the behavior of a metalloenzyme.

4 the mechanism of superoxide reduction by the metalloenzyme.

5 honoacetate hydrolase is also a two-zinc ion metalloenzyme.

6 catalytic mechanism of this quorum-quenching metalloenzyme.

7 Urease is a ubiquitous nickel metalloenzyme.

8 reaction regulated by carbonic anydrase (CA) metalloenzyme.

9 ctive for MBLs when compared to other Zn(II) metalloenzymes.

10 ically relevant carbonic anhydrase (CA) zinc metalloenzymes.

11 herent reactivity of metal centres in native metalloenzymes.

12 s to expand cofactor diversity in artificial metalloenzymes.

13 not catalysed by native Fe-enzymes or other metalloenzymes.

14 files that can be truly unique to artificial metalloenzymes.

15 ets of proteins that defend their vulnerable metalloenzymes.

16 and highlights a possible mode of action for metalloenzymes.

17 and deliver Cu(+) to target transporters or metalloenzymes.

18 nt is the key to uncovering the mechanism of metalloenzymes.

19 te structures of acutely radiation-sensitive metalloenzymes.

20 usible way to reduce promiscuous activity of metalloenzymes.

21 electron transfer in P450 enzymes and other metalloenzymes.

22 cularly involved in drug discovery targeting metalloenzymes.

23 re essential components of cofactors of many metalloenzymes.

24 teins including light-activated switches and metalloenzymes.

25 tion pathways that are analogous to those of metalloenzymes.

26 to be a key intermediate in numerous nonheme metalloenzymes.

27 eral mechanism of regulating the activity of metalloenzymes.

28 rials to understanding catalytic activity of metalloenzymes.

29 The present results can be extended to other metalloenzymes.

30 is of heavy metals and delivery of copper to metalloenzymes.

31 stitute for iron in activating at least some metalloenzymes.

32 ce both the structure and function of native metalloenzymes.

33 hestrating catalytic activity, especially in metalloenzymes.

34 a rare cofactor that is not used by natural metalloenzymes.

35 ilitating efficient drug discovery targeting metalloenzymes.

36 observed in several nucleic-acid-processing metalloenzymes.

37 vanadium (V) and iron (Fe)-only nitrogenase metalloenzymes.

38 can advance our mechanistic understanding of metalloenzymes.

39 secondary coordination sphere influences in metalloenzymes.

40 acterized radical S-adenosylmethionine (RaS) metalloenzymes.

41 nTDMS to characterize complex membrane-bound metalloenzymes.

42 and products to and from the active site in metalloenzymes.

43 iscrimination at the buried metal centers of metalloenzymes.

44 A range of metalloenzymes achieve these challenging tasks in biolog

45 The ultrafast dynamics of a de novo metalloenzyme active site is monitored using two-dimensi

46 a surrogate of a coordinatively-unsaturated metalloenzyme active site, with utility for selecting co

47 s (MOFs) mimic the electronic environment of metalloenzyme active sites, but little is known about th

48 ase residues in the helical core can perturb metalloenzyme activity through the simple expedient of m

49 nd solution state), permitting regulation of metalloenzyme activity without continuous irradiation.

50 a mechanism for exquisite spatial control of metalloenzyme activity.

51 rginase with the related binuclear manganese metalloenzymes agmatinase and proclavaminic acid amidino

52 The metalloenzyme aminopeptidase P catalyzes the hydrolysis

53 least one radical S-adenosylmethionine (RaS) metalloenzyme and are regulated by quorum sensing.

54 ement that serves as a catalytic cofactor in metalloenzymes and a structural element in proteins invo

55 of several drug discovery efforts focused on metalloenzymes and attempt to map out the current landsc

56 e employed to tune the catalytic activity of metalloenzymes and can thus contribute to the future des

57 points to a new direction for understanding metalloenzymes and designing new biomimetic catalysts.

58 f the metal they complex, a strategy used by metalloenzymes and in catalysis.

59 ragments show impressive inhibition of these metalloenzymes and preferences for different MMPs based

60 Unlike metalloenzymes and related biomimetics, the catalyst pro

61 ly down-regulate copper delivery to secreted metalloenzymes and suggest that proteins involved in met

62 of this research to the field of artificial metalloenzymes and synthetic biology.

63 elating antibiotic that inhibits a subset of metalloenzymes and that RNA polymerase is unlikely to be

64 We show here that ARD1 is an active metalloenzyme, and AGB1 and ARD1 both control embryonic

65 ring use of tailored nanoparticles, purified metalloenzyme, and synchrotron X-ray absorption spectros

66 turally occurring iron- or copper-containing metalloenzymes, and extensive studies have revealed the

67 Metalloenzymes are attractive targets for therapeutic in

68 improving the knowledge of how these complex metalloenzymes are biosynthesized.

69 Metalloenzymes are central to a wide range of essential

70 This study tested whether nonredox metalloenzymes are commonly charged with iron in vivo an

71 The active sites of metalloenzymes are often deeply buried inside a hydropho

72 We propose that Mn-metalloenzymes are particularly susceptible to hyperacti

73 features that dictate the metal utilized by metalloenzymes are poorly understood, limiting our abili

74 Nitrile hydratase metalloenzymes are unique and important biocatalysts tha

75 Copper-dependent metalloenzymes are widespread throughout metabolic pathw

76 a protein scaffold to generate an artificial metalloenzyme (ArM) has been explored since the late 197

77 Artificial metalloenzymes (ArMs) are hybrid catalysts that offer a

78 Artificial metalloenzymes (ArMs) formed by incorporating synthetic

79 remote substituents, catalyzed by artificial metalloenzymes (ArMs) that are generated from the combin

80 extensively exploited to engineer artificial metalloenzymes (ArMs) that catalyze a dozen different re

81 Reliable design of artificial metalloenzymes (ArMs) to access transformations not obse

82 on-producing what is known in the context of metalloenzymes as an 'entatic' state-might be a useful w

83 prise studies of both natural and engineered metalloenzymes as well as synthetic model complexes.

84 osynthetic gene clusters that encode unusual metalloenzymes, as these may install as yet unknown alte

85 ucture of the complex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing su

86 ression of many diseases and, as such, makes metalloenzymes attractive targets for therapeutic interv

87 dens our understanding on the mechanisms for metalloenzyme biosynthesis in the presence of oxygen.

88 AurF is a metalloenzyme, but its native enzymatic activity has not

89 y species in the catalytic cycles of nonheme metalloenzymes, but their chemical properties and reacti

90 lyzed by both molecular electrocatalysts and metalloenzymes, but well-defined examples of paramagneti

91 can mimic some of the remarkable features of metalloenzymes by binding substrates in proximity to a b

92 l that function has evolved in these related metalloenzymes by strategically placing very few residue

93 the second coordination sphere of artificial metalloenzymes by using genetic modifications of the pro

94 is a member of the well established class of metalloenzymes called "Radical-SAM." These enzymes use a

95 this reaction under ambient conditions using metalloenzymes called methane monooxygenases (MMOs).

96 global structures and chemical properties of metalloenzymes can be obtained concurrently, providing i

97 ntrol reactivity and selectivity, artificial metalloenzymes can modulate both the first and second co

98 hat the combination of photosensitizers with metalloenzymes can support a light-driven multielectron

99 logically relevant human (h) isoforms of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1).

100 re prepared and assayed as inhibitors of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1).

101 ups (ZBGs) are reported as inhibitors of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1).

102 low micromolar binding affinity to the zinc metalloenzyme carbonic anhydrase II (CA II).

103 In nature, the zinc metalloenzyme carbonic anhydrase II (CAII) efficiently c

104 Redox active metalloenzymes catalyse a range of biochemical processes

105 the action of antioxidants to industrial and metalloenzyme catalysis.

106 tion, energy conversion, photosynthesis, and metalloenzyme catalysis.

107 Metalloenzymes catalyze complex and essential processes,

108 The resulting metalloenzyme catalyzes the hydration of CO2 better than

109 de oxidoreductase (DPOR), a nitrogenase-like metalloenzyme, catalyzes the chemically challenging two-

110 g power) of reactive oxygen intermediates in metalloenzyme chemical system mediated oxidative process

111 Thus, metalloenzyme chemistry is shown to be tuned by the seco

112 ired by the reactivity of these Cu-dependent metalloenzymes, chemists have developed synthetic protoc

113 llide a by the nitrogenase-like multisubunit metalloenzyme, chlorophyllide a oxidoreductase (COR).

114 onversion of CO and CO(2) Like other complex metalloenzymes, CODH requires dedicated assembly machine

115 Artifical metalloenzymes combine the reactivity of small molecule

116 ygenase (pMMO), a copper-dependent, membrane metalloenzyme composed of subunits PmoA, PmoB, and PmoC.

117 tion of metal affinity to the active site of metalloenzymes constitutes an integral part in the under

118 Here, we report a reconstituted artificial metalloenzyme containing an iridium porphyrin that exhib

119 GH61s have already been shown to be unique metalloenzymes containing an active site with a mononucl

120 reveals necessary design features for future metalloenzymes containing one or more metals.

121 Mutations in the metalloenzyme copper-zinc superoxide dismutase (SOD1) ca

122 rent density suggest the advantages of using metalloenzymes covalently attached to polymer-functional

123 ranylgeranyl diphosphate synthase (GGPPS), a metalloenzyme crucial for cell survival.

124 lly analogous to the active site pocket of a metalloenzyme, demonstrating that both the active site a

125 on the recent examples of oxygen-activating metalloenzymes, developed through the strategies of de n

126 The resulting artificial metalloenzyme displays significantly improved catalytic

127 e, 293 cells transfected with JAB1/MPN/Mov34 metalloenzyme domain-deleted CSN5 produced exosomes with

128 somal proteins in both a CSN5 JAB1/MPN/Mov34 metalloenzyme domain-dependent and -independent manner.

129 BRCC36 is a JAMM (JAB1/MPN/Mov34 metalloenzyme) domain, lysine 63-ubiquitin (K63-Ub)-spec

130 of many members of the OTU and JAB/MPN/Mov34 metalloenzyme DUB families and highlight that all USPs t

131 ved reactivity trends reported in artificial metalloenzymes employing iron porphyrin carbenes.

132 bility for polymeric catalysts as artificial metalloenzymes, especially as it relates to bioapplicati

133 or halogenation is increasing, revealing new metalloenzymes, flavoenzymes, S-adenosyl-L-methionine (S

134 ate highly active, productive, and selective metalloenzymes for abiological reactions.

135 d their variants, but also can result in new metalloenzymes for biotechnological and pharmaceutical a

136 Metal clusters are exploited by numerous metalloenzymes for catalysis, but it is not common to ut

137 nases are the best known naturally occurring metalloenzymes for hydrogen generation, and small-molecu

138 Here we show that SznF, a metalloenzyme from the biosynthesis of streptozotocin, c

139 hemical characterization of oxygen-sensitive metalloenzymes from strictly anaerobic species in the Ar

140 rical contact to the metal center of a redox metalloenzyme, galactose oxidase (GOase), by coordinatio

141 Moreover, this homodimeric metalloenzyme has been directly linked to both familial

142 , the scope of reactions catalysed by native metalloenzymes has been expanded recently to include abi

143 s the cofactor compared to Zn(2+)-LpxC; both metalloenzymes have a bell-shaped dependence on pH with

144 udy provides evidence that the metal ions in metalloenzymes have a crucial impact on the catalytic me

145 These metalloenzymes have a large distribution in nature, wher

146 Although artificial metalloenzymes have been developed that catalyze abiolog

147 arly 2000's, different aspects of artificial metalloenzymes have been extensively reviewed and highli

148 tics of the active site (H-cluster) of these metalloenzymes have been synthesized for years.

149 Artificial metalloenzymes have received increasing attention over t

150 reviously identified as a mononuclear Zn(II) metalloenzyme; however, LpxC is 6-8-fold more active wit

151 ineurin-like phosphoesterase (CLP) family of metalloenzymes; however, it cleaves a pyrophosphate bond

152 The binuclear manganese metalloenzyme human arginase I (HAI) is a potential prot

153 Catalysis by the zinc metalloenzyme human carbonic anhydrase II (HCA II) is li

154 tep of CO(2) hydration catalyzed by the zinc-metalloenzyme human carbonic anhydrase II, the binding o

155 und transition metals in the active sites of metalloenzymes if left unregulated.

156 ture as well as the postulated roles of this metalloenzyme in host-pathogen interactions.

157 We also describe an XNA-XNA ligase metalloenzyme in the FANA framework, establishing cataly

158 yl diphosphate synthase (GGPPS) is a central metalloenzyme in the mevalonate pathway, crucial for the

159 rt the creation of a bifunctional artificial metalloenzyme in which a glutamic acid or aspartic acid

160 c study of hydrides in a variety of reducing metalloenzymes in addition to nitrogenase.

161 ethodology for structure/function studies of metalloenzymes in general.

162 gy for improving the catalytic efficiency of metalloenzymes in the context of abiological transformat

163 zyme cofactor is built and the role of these metalloenzymes in the physiology of the organism.

164 The role of metalloenzymes in these processes also makes them centra

165 acting as a cofactor for several enzymes and metalloenzymes, in addition to playing a role in immune

166 A panel of metalloenzymes, including carbonic anhydrase (hCAII), se

167 -compatible platform, which could accelerate metalloenzyme inhibitor discovery.

168 nhibitory activity of a broad group of known metalloenzyme inhibitors against a panel of metalloenzym

169 The results show that the metalloenzyme inhibitors are quite selective for their i

170 t can be used to design potent and selective metalloenzyme inhibitors in various therapeutic areas.

171 e results suggest that metal coordination by metalloenzyme inhibitors is a malleable interaction and

172 to reversibly bind experimental or clinical metalloenzyme inhibitors of Zn(II)-ACE1, Zn(II)-HDAC, Fe

173 e utilized universally in the development of metalloenzyme inhibitors, they are considered to be poor

174 e metal-binding group (MBG) in this class of metalloenzyme inhibitors.

175 al-binding groups from mixtures as potential metalloenzyme inhibitors.

176 at Crocosphaera's ability to reduce its iron-metalloenzyme inventory provides two advantages: It allo

177 ir utilization results in a lowered cellular metalloenzyme inventory that requires approximately 40%

178 Tyrosinase is a metalloenzyme involved in o-hydroxylation of monophenols

179 Alterations in the assembly of metalloenzymes involved in redox stress response might e

180 Synthesis of these metalloenzymes involves a complex series of biochemical

181 ird strategy, in which the native metal of a metalloenzyme is replaced with an abiological metal with

182 Thus, metallation of an estimated 30% of metalloenzymes is aided by metal delivery systems, with

183 e understanding of the native cofactor(s) of metalloenzymes is critical for the development of biolog

184 Proteins with JAB1/MPN/MOV34 metalloenzyme (JAMM/MPN+) domains are widespread among a

185 We created a Metalloenzyme-Ligand Association Database (MeLAD), which

186 3726 and 52 740 deductive metalloenzyme-ligand associations by MeSIM and LigSIM an

187 zed, interconnected information exclusive to metalloenzyme-ligand associations.

188 The fast-growing body of structural data on metalloenzyme-ligand interactions is facilitating effici

189 structural data and information exclusive to metalloenzyme-ligand interactions, and more uniquely, pr

190 The use of metalloenzyme-like zeolites as Lewis acid catalysts for

191 These results may shed light on how a metalloenzyme maintains its catalytic activity in an oxi

192 extended H-bond networks in designing other metalloenzymes may allow us to confer and fine-tune thei

193 licofelone, demonstrating a remarkable IMAC-metalloenzyme metal ion match.

194 we report that the membrane-tethered matrix metalloenzyme MT1-MMP not only serves as an ECM-directed

195 LAD is searchable by multiple criteria, e.g. metalloenzyme name, ligand identifier, functional class,

196 apid antibiotic-mediated evolution of a zinc metalloenzyme obligatorily occurs in the context of host

197 atase/diesterase, a promiscuous two-zinc ion metalloenzyme of the alkaline phosphatase enzyme superfa

198 Arginase, a key metalloenzyme of the urea cycle that converts L-arginine

199 Metalloenzymes often require elaborate metallocenter ass

200 Why metalloenzymes often show dramatic changes in their cata

201 d to prepare other Co(II)-substituted Zn(II)-metalloenzymes, particularly those that contain a solven

202 Increasing awareness of the role metalloenzymes play in disease and their importance as a

203 Enzymes that contain metal ions--that is, metalloenzymes--possess the reactivity of a transition m

204 Carbonic anhydrases (CAs; EC 4.2.1.1) are metalloenzymes present in mammals with 16 isoforms that

205 rticulate MMO (pMMO) is an integral membrane metalloenzyme produced by all methanotrophs and is compo

206 line server is provided for users to conduct metalloenzyme profiling prediction for small molecules o

207 The metalloenzyme protein phosphatase 1 (PP1), which is resp

208 d hydrogen bonding structures in a bona fide metalloenzyme proton pathway.

209 cies is critical to both an understanding of metalloenzyme reactivity and related transition metal ca

210 valuable, integrative data source to foster metalloenzyme related research, particularly involved in

211 Metalloenzymes rely on earth-abundant metals to perform

212 drase XII (CA12), a gene that encodes a zinc metalloenzyme responsible for acidification of the micro

213 RNase P is the ubiquitous ribonucleoprotein metalloenzyme responsible for cleaving the 5'-leader seq

214 RPE65 is a key metalloenzyme responsible for maintaining visual functio

215 Artificial metalloenzymes result from anchoring an active catalyst

216 of reduced holomycin against zinc-dependent metalloenzymes revealed that it inhibits E. coli class I

217 is of this first de novo designed hydrolytic metalloenzyme reveals necessary design features for futu

218 e approach to the construction of artificial metalloenzymes since this is conveniently achieved by se

219 Thus, PDS readily detects alterations in metalloenzyme solution properties not easily deciphered

220 nted by metal-binding pharmacophores (MBPs), metalloenzyme structural similarity (MeSIM) and ligand c

221 catalysts provide processing advantages over metalloenzymes such as an ability to work at higher temp

222 amily comprises a large number of hydrolytic metalloenzymes such as phosphatases and sulfatases.

223 ity of oxygen-containing metal complexes and metalloenzymes, such as the oxygen-evolving complex in p

224 een linked with mutations to the antioxidant metalloenzyme superoxide dismutase (SOD1).

225 the catalytic roles of metal ions in a model metalloenzyme system, human carbonic anhydrase II (CA II

226 ethyl-l-arginine (l-NMA) by the multi-domain metalloenzyme SznF.

227 other metal ions could broaden the scope of metalloenzyme target.

228 map out the current landscape of high-value metalloenzyme targets.

229 disintegrin and metalloprotease (ADAM) 17, a metalloenzyme that catalyzes ectodomain shedding of rece

230 Nitrogenase is an essential metalloenzyme that catalyzes the biological conversion o

231 minopeptidase (LTA4H) is a bifunctional zinc metalloenzyme that catalyzes the committed step in the f

232 ) is a mononuclear cysteinate-ligated nickel metalloenzyme that catalyzes the disproportionation of s

233 A desaturase 1 (SCD1) is a membrane-embedded metalloenzyme that catalyzes the formation of a double b

234 e II (HCA II) is a monomeric zinc-containing metalloenzyme that catalyzes the hydration of CO(2) to f

235 monooxygenase (pMMO) is an integral membrane metalloenzyme that converts methane to methanol in metha

236 Superoxide reductase is a nonheme iron metalloenzyme that detoxifies superoxide anion radicals

237 superoxide dismutase (SOD) is a homodimeric metalloenzyme that has been extensively studied as a ben

238 csG) is a predicted inner membrane-localized metalloenzyme that has been proposed to catalyze the tra

239 extracellular transmembrane homodimeric zinc metalloenzyme that has been validated as a prognostic ma

240 Nitrogenase is a versatile metalloenzyme that is capable of catalyzing two importan

241 egraded by dihydropyrimidinase (DHP), a zinc metalloenzyme that is upregulated in solid tumors but no

242 bdenum cofactor (Moco)-dependent homodimeric metalloenzyme that is vitally important for autotrophic

243 ane monooxygenase (pMMO) is a membrane-bound metalloenzyme that oxidizes methane to methanol in metha

244 Arginase is a binuclear manganese metalloenzyme that serves as a therapeutic target for th

245 This enzyme is an Mg(2+)/Mn(2+)-dependent metalloenzyme that undergoes dramatic activation upon re

246 teine methyltransferase-2 (BHMT-2) is a zinc metalloenzyme that uses S-methylmethionine (SMM) as a me

247 ve obligate requirements for trace metals in metalloenzymes that catalyse important biogeochemical re

248 Hydrogenases are metalloenzymes that catalyze 2H(+) + 2e(-) <--> H(2).

249 u(2+), has been harnessed by a wide array of metalloenzymes that catalyze electron transfer reactions

250 Here, metalloenzymes that catalyze the cleavage of this chemic

251 Hydrogenases are metalloenzymes that catalyze the conversion of protons a

252 Carbonic anhydrases (CAs) are zinc metalloenzymes that catalyze the interconversion of CO2

253 [NiFe] hydrogenases are metalloenzymes that catalyze the reversible oxidation of

254 Hydrogenases are metalloenzymes that catalyze the reversible oxidation of

255 Consequently, all hydrogenases are metalloenzymes that contain at least one iron atom in th

256 Inspired by natural metalloenzymes that efficiently catalyze a variety of tr

257 a novel design for supramolecular artificial metalloenzymes that exploits the promiscuity of the cent

258 that are essential to life are catalyzed by metalloenzymes that feature Earth-abundant metals.

259 ossible role of unusually low valent iron in metalloenzymes that feature iron-sulfur clusters.

260 o isatinate and belongs to a novel family of metalloenzymes that include the bacterial kynurenine for

261 Carbonic anhydrases (CAs) are zinc metalloenzymes that interconvert CO2 and HCO3 (-) In pla

262 Metalloenzymes that often exhibit this type of reactivit

263 Sulfite oxidases are metalloenzymes that oxidize sulfite to sulfate at a moly

264 n-binding scaffolds can be adapted to obtain metalloenzymes that provide the reactivity of the introd

265 atom abstraction in thiolate-ligated nonheme metalloenzymes that react with O(2).

266 Oxygen-tolerant [NiFe] hydrogenases are metalloenzymes that represent valuable model systems for

267 Although cells express hundreds of metalloenzymes, the mechanisms by which apoenzymes recei

268 In redox metalloenzymes, the process of electron transfer often i

269 The key metalloenzyme to degrade ROS in B. burgdorferi is SodA.

270 The ability of many copper metalloenzymes to activate O2 and transfer it to organic

271 potential of abiotic reactions catalyzed by metalloenzymes to functionalize C-H bonds with site sele

272 he understanding of biological processes and metalloenzymes to the development of inorganic catalysts

273 The triphosphate tunnel metalloenzyme (TTM) superfamily represents a group of en

274 Triphosphate tunnel metalloenzymes (TTMs) are a superfamily of phosphotransf

275 Triphosphate tunnel metalloenzymes (TTMs) are present in all kingdoms of lif

276 Inhibitors of metalloenzymes typically contain a group that binds to t

277 uman stomach, requires the nickel-containing metalloenzymes urease and NiFe-hydrogenase to survive th

278 idized and reduced forms of this 414-residue metalloenzyme via hydrogen-deuterium exchange kinetics (

279 the structure and physical properties of the metalloenzyme vs the NiSOD metallopeptide-based models.

280 The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography.

281 of nature's approach to catalysis, a Zn(II) metalloenzyme was prepared using de novo design.

282 metalloenzyme inhibitors against a panel of metalloenzymes was evaluated.

283 s enzyme, which has the characteristics of a metalloenzyme, was purified approximately 200-fold from

284 ch enzyme is the human exonuclease 1 (hExo1) metalloenzyme, which cleaves DNA strands, acting primari

285 se of its central role in the functioning of metalloenzymes, which utilize O2 to perform a number of

286 mes do not synthesize an active Zn(II)-bound metalloenzyme, while the as-isolated ribosomes do.

287 reminiscent of MiaB, another tRNA-modifying metalloenzyme whose active form was shown to bind two ir

288 The rational design of inhibitors targeting metalloenzymes will benefit greatly from a deeper unders

289 e factors that govern the properties of this metalloenzyme with a goal of eventually improving the ca

290 erization revealed that NaaA is a hydrolytic metalloenzyme with a narrow substrate range.

291 ron catalytic site; pMMO is a membrane-bound metalloenzyme with a unique tricopper cluster as the sit

292 6 structurally resolved interactions of 1416 metalloenzymes with 3564 ligands, of which classical met

293 being made in the design and engineering of metalloenzymes with catalytic properties fulfilling the

294 ependent activity can drive the evolution of metalloenzymes with new cofactor specificity.

295 OX-like (LOXL) proteins are copper-dependent metalloenzymes with well-documented roles in tumor metas

296 verse micelle (ICRM) produced an artificial "metalloenzyme" with highly unusual catalytic properties.

297 carboxypeptidases (CCPs) are a subfamily of metalloenzymes within the larger M14 family of carboxype

298 ATP7A transfers the copper cofactor to metalloenzymes within the secretory pathway; inactivatio

299 to bind zinc, and these metals dominate the metalloenzymes without metal delivery systems.

300 some enzymes that are not recognized as zinc metalloenzymes, zinc binding inhibits rather than activa