Crystal Structure of D-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability (Q27641581)

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Language	Label	Description	Also known as
English	Crystal Structure of D-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability	scientific article

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scholarly article

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Crystal Structure of D-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability (English)

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crystal structure

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Burkholderia pickettii

object named as

Burkholderia pickettii

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based on heuristic

inferred from title

5

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author name string

Zhen Xu

1

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Yunqing Liu

2

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Yunliu Yang

3

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Weihong Jiang

4

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Jianping Ding

6

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language of work or name

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publication date

July 2003

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Journal of Bacteriology

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185

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14

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4038-49

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Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability

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Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids

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Homology modeling reveals the structural background of the striking difference in thermal stability between two related [NiFe]hydrogenases

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Protein thermal stability, hydrogen bonds, and ion pairs

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Identifiers

10.1128/JB.185.14.4038-4049.2003

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