Thermal stability of methanol dehydrogenase is altered by the replacement of enzyme-bound Ca2+ with Sr2+.

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Thermal stability of methanol dehydrogenase is altered by the replacement of enzyme-bound Ca2+ with Sr2+.

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1994 nî lūn-bûn

@nan

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

1994年论文

@zh

1994年论文

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Thermal stability of methanol ...... f enzyme-bound Ca2+ with Sr2+.

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Thermal stability of methanol ...... f enzyme-bound Ca2+ with Sr2+.

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Thermal stability of methanol ...... f enzyme-bound Ca2+ with Sr2+.

@en

P1476

Thermal stability of methanol ...... f enzyme-bound Ca2+ with Sr2+.

@en

P2093

T K Harris

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V L Davidson

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P2860

A novel coenzyme from bacterial primary alcohol dehydrogenases

The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1.

Reversible thermal inactivation of the quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Ca2+ ions are necessary for re-activation.

Replacement of enzyme-bound calcium with strontium alters the kinetic properties of methanol dehydrogenase.

Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion.

A new kinetic model for the steady-state reactions of the quinoprotein methanol dehydrogenase from Paracoccus denitrificans.

P304

141-145

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P31

scholarly article

P356

10.1042/BJ3030141

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P407

English

P478

303 ( Pt 1)

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P577

1994-10-01T00:00:00Z

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P5875

15254470

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P698

7945232

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P932

1137568

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