A substate-induced conformation change in the reaction of alkaline phosphatase from Escherichia coli
about
Escherichia coli alkaline phosphatase. Kinetic studies with the tetrameric enzymeEscherichia coli alkaline phosphatase. Relaxation spectra of ligand bindingStopped-flow fluorescence studies on saccharide binding to lysozyme.The mechanism of hydrolysis of beta-glycerophosphate by kidney alkaline phosphatase.Alkaline phosphatase activity in a strain of Bacterionema matruchotii.The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociation.Mutationally altered rate constants in the mechanism of alkaline phosphatase.Escherichia coli alkaline phosphatase. An analysis of transient kinetics.A new class of chromophoric organomercurials and their reactions with D-glyceraldehyde 3-phosphate dehydrogenaseCalcium and the assays of human plasma clotting factor XIII.Kinetic and molecular properties of citraconyl-aldolase. The reversible denaturation and hybridization of the native and modified enzymes.The Cu2 plus-alkaline phosphatase of Escherichia coli.Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics. A choice of models.Dimer asymmetry and the catalytic cycle of alkaline phosphatase from Escherichia coli.The functional properties of the Zn2(plus)-and Co2(plus)-alkaline phosphatases of Escherichia coli. Labelling of the active site with pyrophosphate, complex formation with arsenate, and reinvestigation of the role of the zinc atoms.Reaction Kinetics of the Invertase from Yeast (S. Cerevisiae)
P2860
Q28363524-5B146032-4BC3-4282-99E7-EF6D48274106Q28363527-17943804-2D88-42CD-B03E-C72A52F5BE59Q38360245-DB2FF089-5FE6-45CE-B8E6-3B3E2F2693E6Q39066656-8CB9478D-7C0D-41A4-81C7-F9DDEDFDF01CQ40595799-607FEDF4-0585-45B7-BDDC-08AEAAA1FE32Q41769868-B753876D-B916-4633-87BD-0EB78E6DAA75Q41870473-FF20F6CA-9795-487D-A54C-A8CCA45D960DQ42080143-A3F93E35-6F1C-4D14-8681-ED4DA489022BQ42096223-41E456E5-7690-42E3-BB3F-92F0380708E9Q42236522-0927EC2D-33A1-4B76-AA88-7E0B93420764Q42561990-A349746B-7E63-447F-A81E-5D464A51365AQ43462255-D88747D3-3A98-4200-9E58-2E8343E146AAQ44821709-F332A280-9A18-45A9-896C-7936B63EE5D8Q47380511-AED1703F-C25D-4FAB-802E-2EF490840C31Q54246859-D7651A75-F8F2-4FB1-829D-6A2BA457B872Q58337141-453A9A92-3A9E-4C81-BEC8-6C2C15065EA3
P2860
A substate-induced conformation change in the reaction of alkaline phosphatase from Escherichia coli
description
1969 nî lūn-bûn
@nan
1969年の論文
@ja
1969年論文
@yue
1969年論文
@zh-hant
1969年論文
@zh-hk
1969年論文
@zh-mo
1969年論文
@zh-tw
1969年论文
@wuu
1969年论文
@zh
1969年论文
@zh-cn
name
A substate-induced conformatio ...... sphatase from Escherichia coli
@en
type
label
A substate-induced conformatio ...... sphatase from Escherichia coli
@en
prefLabel
A substate-induced conformatio ...... sphatase from Escherichia coli
@en
P2093
P2860
P356
P1433
P1476
A substate-induced conformatio ...... sphatase from Escherichia coli
@en
P2093
D R Trentham
H Gutfeund
N G Bennett
S E Halford
P2860
P304
P356
10.1042/BJ1140243
P407
P577
1969-09-01T00:00:00Z