Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.

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Hydroxamic acids as potent inhibitors of Fe(II) and Mn(II) E. coli methionine aminopeptidase: biological activities and X-ray structures of oxazole hydroxamate-EcMetAP-Mn complexes Self-subunit swapping occurs in another gene type of cobalt nitrile hydratase

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P2860

Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.

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http://www.wikidata.org/entity/Q37234265

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2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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name

Analyzing the catalytic role o ...... ptidase from Escherichia coli.

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Analyzing the catalytic role o ...... ptidase from Escherichia coli.

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type

Item

label

Analyzing the catalytic role o ...... ptidase from Escherichia coli.

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Analyzing the catalytic role o ...... ptidase from Escherichia coli.

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Analyzing the catalytic role o ...... ptidase from Escherichia coli.

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Analyzing the catalytic role o ...... ptidase from Escherichia coli.

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P1476

Analyzing the catalytic role o ...... eptidase from Escherichia coli

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P2093

Brian Bennett

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Lu Meng

http://www.w3.org/2001/XMLSchema#string

Richard C Holz

http://www.w3.org/2001/XMLSchema#string

Sanghamitra Mitra

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P2860

The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase

Methionine aminopeptidase gene of Escherichia coli is essential for cell growth

The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2

Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis

Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus

Structure of human methionine aminopeptidase-2 complexed with fumagillin

Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.

Metalloaminopeptidases: common functional themes in disparate structural surroundings

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scholarly article

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10.1111/J.1742-4658.2008.06749.X

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English

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275

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Kathleen M Job

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2008-11-13T00:00:00Z

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23483156

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19019076

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2699115

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Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.

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P2860

P2860

Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.

description

name

type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932

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P1476

P2093

P2860

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P356

P407

P433

P478

P50

P577

P5875

P698

P932