Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids.
about
Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostabilityStructural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridgingEnantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coliStructural and functional properties of a yeast xylitol dehydrogenase, a Zn2+-containing metalloenzyme similar to medium-chain sorbitol dehydrogenases.An unusual oxygen-sensitive, iron- and zinc-containing alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosusMechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis.The conserved Glu-60 residue in Thermoanaerobacter brockii alcohol dehydrogenase is not essential for catalysis.Bioaffinity purification of NADP(+)-dependent dehydrogenases: studies with alcohol dehydrogenase from Thermoanaerobacter brockii.Cysteine reactivity in Thermoanaerobacter brockii alcohol dehydrogenase.Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase.Determining the roles of the three alcohol dehydrogenases (AdhA, AdhB and AdhE) in Thermoanaerobacter ethanolicus during ethanol formation.Practical two-step synthesis of enantiopure styrene oxide through an optimized chemoenzymatic approach.A Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase mutant derivative highly active and stereoselective on phenylacetone and benzylacetone.Substitution of the catalytic metal and protein PEGylation enhances activity and stability of bacterial phosphotriesterase.Biochemical characterization of an alcohol dehydrogenase fromRalstoniasp
P2860
Q27621093-D6F77CD2-3953-49FB-80C9-341D68330246Q27639831-6B68E57E-03F7-4F7B-B075-C41577C36E0BQ27701467-32FE1B2D-154C-4FE9-9905-0F1E1DF2AB0BQ31979159-AF17404A-A207-4796-ADF3-95BDEC2F7482Q33991250-147797AB-4A98-42CA-A416-F03529CF902DQ35181375-9C4AF116-6FAA-424D-AE53-6B6EA9B9EBA3Q36559814-44A14DE8-A405-4B6E-8BC7-F2BFE187DCC4Q40666708-165E4B84-4671-4CBE-8076-28F9F45B4D56Q42845857-EFC7C64F-919A-4A8A-A30A-E11FADD38067Q42846464-228F4707-DD6B-46C0-8957-964DEBDF3817Q43029466-22F7FFB2-291D-45CD-A2CD-BB764625C8BCQ50849529-133A8AE5-FD3F-4D0D-A62C-D00FF216C1E7Q51068732-1EE42CDC-8FAD-43E6-B2FE-85E2BFC09BF4Q54344162-AEAD32AE-21A3-404B-9F43-EFBA427F2B68Q58942860-8AF5DE00-4BB0-4EB4-AE4A-725F2ADE420A
P2860
Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Thermoanaerobacter brockii alc ...... al and its ligand amino acids.
@en
type
label
Thermoanaerobacter brockii alc ...... al and its ligand amino acids.
@en
prefLabel
Thermoanaerobacter brockii alc ...... al and its ligand amino acids.
@en
P2093
P2860
P356
P1433
P1476
Thermoanaerobacter brockii alc ...... al and its ligand amino acids.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560060223
P577
1997-02-01T00:00:00Z