(Q27766346)

English

1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and correlation with inherited deficiency

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scholarly article

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1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and correlation with inherited deficiency (English)

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crystal structure

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author name string

D Shi

1

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H Morizono

2

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Y Ha

3

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M Aoyagi

4

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M Tuchman

5

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N M Allewell

6

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language of work or name

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publication date

18 December 1998

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Journal of Biological Chemistry

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273

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51

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34247-54

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The biochemical and molecular spectrum of ornithine transcarbamylase deficiency.

1 reference

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1 reference

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AMoRe: an automated package for molecular replacement

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Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures.

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Site-directed mutagenesis of Arg60 and Cys271 in ornithine transcarbamylase from rat liver

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The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study.

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YMC1, a yeast gene encoding a new putative mitochondrial carrier protein.

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Analysis of a 70 kb region on the right arm of yeast chromosome II.

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ALSCRIPT: a tool to format multiple sequence alignments

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Aspartate transcarbamylase from Escherichia coli: activity and regulation

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Effects of pH on the kinetics of human liver ornithine-carbamyl phosphate transferase

1 reference

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Characterization of two ornithine carbamoyltransferases from Pseudomonas syringae pv. phaseolicola, the producer of phaseolotoxin.

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Identifiers

10.1074/JBC.273.51.34247

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