The structure of bovine liver rhodanese. II. The active site in the sulfur-substituted and the sulfur-free enzyme.
about
NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditionsThe crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active siteCrystal structure of YnjE fromEscherichia coli, a sulfurtransferase with three rhodanese domainsS-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family ProteinActive site structural features for chemically modified forms of rhodaneseY13C Azotobacter vinelandii ferredoxin I. A designed [Fe-S] ligand motif contains a cysteine persulfideBiosynthesis of a central intermediate in hydrogen sulfide metabolism by a novel human sulfurtransferase and its yeast orthologPlant mercaptopyruvate sulfurtransferases: molecular cloning, subcellular localization and enzymatic activities.The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relationsChemical foundations of hydrogen sulfide biology.Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. CDNA cloning, overexpression, and site-directed mutagenesis.Catalytic site cysteines of thiol enzyme: sulfurtransferases.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.Chemical Biology of H2S Signaling through Persulfidation.Conformational studies on Arabidopsis sulfurtransferase AtStr1 with spectroscopic methods.Conservation of amino acids in multiple alignments: aspartic acid has unexpected conservation
P2860
Q27618135-11833A82-2C93-4FE8-970A-BB4DFB23CF3BQ27641943-7F972018-F8E3-48BD-8105-EC44764E0B69Q27657637-F43EB727-FB98-4C26-B469-53F3E1FFDB13Q27722821-8CF8B26E-16F1-4C40-8D5C-1FB6C50B7CD7Q27733198-A0691E89-5D04-4759-80AC-60A83BC565C9Q27739255-B716421F-F7CB-48E9-ABCB-A0BF91B1944CQ27930143-5A8D6144-06FE-4787-966E-4BE1A72D0458Q30908299-43669EA4-B1BB-4C86-8338-9471E4233BBAQ33758088-92AABF4F-0B64-44DB-95F6-319C0347E65BQ38121347-0343AAD9-AA56-417C-9A21-2F18BA40C6E6Q38351941-D48F4DE4-8C4D-403C-875C-43BC7BA5ADD9Q40973262-8DE47189-82EE-4BAA-8FAE-CE34C7D700FCQ44219935-64584DBC-6974-424A-891D-D9CE23938E41Q47430972-E65F1CFC-D3E2-4BC8-9E8F-97D8E5F5DF11Q54448756-C3FB9F1F-F68C-4C64-92B8-3FF8BDBD423CQ57065043-A732EECF-E706-4759-AFAB-AB7FA5321BD9
P2860
The structure of bovine liver rhodanese. II. The active site in the sulfur-substituted and the sulfur-free enzyme.
description
1979 nî lūn-bûn
@nan
1979年の論文
@ja
1979年論文
@yue
1979年論文
@zh-hant
1979年論文
@zh-hk
1979年論文
@zh-mo
1979年論文
@zh-tw
1979年论文
@wuu
1979年论文
@zh
1979年论文
@zh-cn
name
The structure of bovine liver ...... ed and the sulfur-free enzyme.
@en
type
label
The structure of bovine liver ...... ed and the sulfur-free enzyme.
@en
prefLabel
The structure of bovine liver ...... ed and the sulfur-free enzyme.
@en
P2093
P1476
The structure of bovine liver ...... ed and the sulfur-free enzyme.
@en
P2093
P304
P356
10.1016/0022-2836(79)90236-5
P407
P577
1979-01-01T00:00:00Z