Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue.
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Structure, mechanism and regulation of pyruvate carboxylaseDomain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzymeCharacterization of a bifunctional archaeal acyl coenzyme A carboxylase.Novel insights into the biotin carboxylase domain reactions of pyruvate carboxylase from Rhizobium etli.Nearly 50 years in the making: defining the catalytic mechanism of the multifunctional enzyme, pyruvate carboxylase.
P2860
Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue.
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1998 nî lūn-bûn
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1998年の論文
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1998年学术文章
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1998年学术文章
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1998年學術文章
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name
Identification of lysine-238 o ...... ase as an ATP-binding residue.
@en
Identification of lysine-238 o ...... ase as an ATP-binding residue.
@nl
type
label
Identification of lysine-238 o ...... ase as an ATP-binding residue.
@en
Identification of lysine-238 o ...... ase as an ATP-binding residue.
@nl
prefLabel
Identification of lysine-238 o ...... ase as an ATP-binding residue.
@en
Identification of lysine-238 o ...... ase as an ATP-binding residue.
@nl
P2093
P2860
P1433
P1476
Identification of lysine-238 o ...... ase as an ATP-binding residue.
@en
P2093
P2860
P304
P356
10.1016/S0014-5793(98)00472-4
P407
P577
1998-05-01T00:00:00Z