(Q27730287)

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Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes

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Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes (English)

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crystal structure

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Isopenicillin-N synthase

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author name string

P L Roach

1

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I J Clifton

2

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V Fülöp

3

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K Harlos

4

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G J Barton

5

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J Hajdu

6

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I Andersson

7

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C J Schofield

8

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J E Baldwin

9

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language of work or name

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publication date

22 June 1995

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375

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6533

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700-4

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Purification of isopenicillin N synthetase

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Crystallization and Preliminary X-ray Diffraction Studies on a Recombinant Isopenicillin N Synthase from Cephalosporium acremonium

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Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans

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[25] Protein multiple sequence alignment and flexible pattern matching

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ALSCRIPT: a tool to format multiple sequence alignments

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Thiolate ligation of the active site Fe2+ of isopenicillin N synthase derives from substrate rather than endogenous cysteine: spectroscopic studies of site-specific Cys----Ser mutated enzymes

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X-ray absorption studies of the ferrous active site of isopenicillin N synthase and related model complexes

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X-ray absorption spectroscopic studies of the high-spin iron(II) active site of isopenicillin N synthase: evidence for Fe-S interaction in the enzyme-substrate complex.

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10.1038/375700A0

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