The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families
about
Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5A conserved mechanism for sulfonucleotide reductionA persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii RhodaneseStructural basis for the oxidation of thiosulfate by a sulfur cycle enzyme.The SoxYZ complex carries sulfur cycle intermediates on a peptide swinging armCrystal Structure and Catalytic Properties of Bacillus anthracis CoADR-RHD: Implications for Flavin-Linked Sulfur TraffickingCrystal structure of YnjE fromEscherichia coli, a sulfurtransferase with three rhodanese domainsStructural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein InteractionsDiscovery and Mechanistic Characterization of Selective Inhibitors of H2S-producing Enzyme: 3-Mercaptopyruvate Sulfurtransferase (3MST) Targeting Active-site Cysteine PersulfideThe N-terminal rhodanese domain from Azotobacter vinelandii has a stable and folded structure independently of the C-terminal domain.Rhodanese-thioredoxin system and allyl sulfur compounds.Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica, but is not required for assembly of its iron-sulfur clusters.The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form.The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relationsInvolvement of the Azotobacter vinelandii rhodanese-like protein RhdA in the glutathione regeneration pathway.Optimization of liposomal lipid composition for a new, reactive sulfur donor, and in vivo efficacy studies on mice to antagonize cyanide intoxicationMetatranscriptomic analysis of a high-sulfide aquatic spring reveals insights into sulfur cycling and unexpected aerobic metabolismCrystallization and preliminary crystallographic characterization of LmACR2, an arsenate/antimonate reductase from Leishmania major.Solution structure of the rhodanese homology domain At4g01050(175-295) from Arabidopsis thaliana.Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN(-) binding defined by EPR-based hybrid method.Latest news about the sulfurtransferase protein family of higher plants.Nanoencapsulated and microencapsulated enzymes in drug antidotal therapy.Possible roles of plant sulfurtransferases in detoxification of cyanide, reactive oxygen species, selected heavy metals and arsenate.Recombinant Escherichia coli with sulfide:quinone oxidoreductase and persulfide dioxygenase rapidly oxidises sulfide to sulfite and thiosulfate via a new pathway.Catalytic site cysteines of thiol enzyme: sulfurtransferases.Biochemical and Genetic Characterization of PspE and GlpE, Two Single-domain Sulfurtransferases of Escherichia coli.The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance.Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition.3-Mercaptopyruvate sulfurtransferase of Leishmania contains an unusual C-terminal extension and is involved in thioredoxin and antioxidant metabolism.Enzymatic activity of the Arabidopsis sulfurtransferase resides in the C-terminal domain but is boosted by the N-terminal domain and the linker peptide in the full-length enzyme.Molecular recognition between Azotobacter vinelandii rhodanese and a sulfur acceptor protein.An unusual tandem-domain rhodanese harbouring two active sites identified in Desulfitobacterium hafniense.Identification of a rhodanese-like protein involved in thiouridine biosynthesis in Thermus thermophilus tRNA.Conformational studies on Arabidopsis sulfurtransferase AtStr1 with spectroscopic methods.Structural basis for the recognition of sulfur in phosphorothioated DNA
P2860
Q24648873-F1EAA5B3-3566-434C-B7EF-C4F21F07D01AQ24811125-D2EDE8C0-5D11-4B76-890D-0741A3619E41Q27635298-3DE99619-9E56-45E5-AB40-9DFB9FCCBC2AQ27639900-1AD820D4-0851-4B1D-8C3A-0F551B6D06EEQ27644861-77BE0FFE-04D7-45AC-9466-FC2A9B1EB5E1Q27657276-9C908041-F906-4C5B-A1CF-6C0A4193CCD6Q27657637-7D89F260-9C70-4BCA-B941-F08F7334D455Q27660665-38D10CDE-0963-4F91-8F21-5BAFE7135D34Q28817472-F0DE9227-7CDB-4817-BB46-E09390BF88E2Q30976835-0B144D80-F1C8-467B-BA98-5840398FD520Q31162170-C3373ECC-1568-48CA-92B7-AA908F98411DQ33227897-8F62E8DF-A7BB-40A3-8F5F-E4AD942598AAQ33227899-8F492298-A805-49D1-8595-D78BCE1EFCF3Q33758088-06007E66-7E71-4C1D-99DF-10AA4A3E45AFQ34438013-D731700F-A45E-435E-984A-E4B314E03208Q35609181-9B72C5F4-10C5-45B3-92BB-05E0FADFE3F3Q35791393-D09C9BEE-8AC6-4B5F-A943-9B34BA6FCDFDQ36426237-97F2CADB-8FE6-403E-B278-7B4EFB077BD1Q36476774-34AAED63-71D4-4EBA-BD66-B859C39D63F1Q36512272-66AA5ECC-11A2-4108-9501-52FF30374ADBQ37687906-DB2A93D1-C0F2-4D36-B6A5-DDA866CFCCEBQ37944132-CE79B7B9-294B-4553-A715-F5C69DD682F7Q38320602-57466223-626D-4ADA-90D3-087707BED19DQ39442166-C5E3D767-5E81-4279-AC96-09492696F776Q40973262-4281E37F-EDC7-4CC8-B6D7-5AA7177D3C61Q41376700-912C5871-2F13-4C58-9201-6166D654AEB5Q43060198-EEF66700-35EF-4D89-AF33-73045C16E17DQ43668044-FC838C01-40DB-4BD6-A54E-955FD3B84CD6Q44207668-A58E605A-68E9-4C90-9FE8-4537BD3A2A01Q44219935-F65303E4-5DF7-4D95-B573-CB96D4063FD2Q44689327-1F83E86E-D067-40AC-BF46-EB1AE80D1D14Q45975631-14B24901-9C04-42D4-B6E1-2EFA7AE6D0D2Q47849527-EE97F88D-9A47-47B2-9937-E4B65C65BA15Q54448756-4969F94E-DD76-4269-8EC8-C8A887B51529Q58586503-C90CE1CC-8732-4A64-8225-FA58B5527F73
P2860
The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families
description
2000 nî lūn-bûn
@nan
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The crystal structure of a sul ...... nd phosphatase enzyme families
@ast
The crystal structure of a sul ...... nd phosphatase enzyme families
@en
The crystal structure of a sul ...... nd phosphatase enzyme families
@nl
type
label
The crystal structure of a sul ...... nd phosphatase enzyme families
@ast
The crystal structure of a sul ...... nd phosphatase enzyme families
@en
The crystal structure of a sul ...... nd phosphatase enzyme families
@nl
prefLabel
The crystal structure of a sul ...... nd phosphatase enzyme families
@ast
The crystal structure of a sul ...... nd phosphatase enzyme families
@en
The crystal structure of a sul ...... nd phosphatase enzyme families
@nl
P2093
P356
P1476
The crystal structure of a sul ...... nd phosphatase enzyme families
@en
P2093
P304
P356
10.1006/JMBI.2000.3651
P407
P577
2000-05-12T00:00:00Z