(Q27733391)

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Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase

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Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase (English)

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crystal structure

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Glutamine Hydroxamate

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ChEBI release 2020-05-28

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1

object named as

M N Isupov

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Alexey Teplyakov

object named as

A Teplyakov

8

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Igor Polikarpov

object named as

I Polikarpov

6

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author name string

G Obmolova

2

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S Butterworth

3

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M A Badet-Denisot

4

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B Badet

5

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J A Littlechild

7

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publication date

15 July 1996

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4

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7

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801-10

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The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families

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Genetic and biomedical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli

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Glucosamine-6-phosphate synthase from Escherichia coli yields two proteins upon limited proteolysis: identification of the glutamine amidohydrolase and 2R ketose/aldose isomerase-bearing domains based on their biochemical properties

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Crystallization and Preliminary X-ray Analysis of the Two Domains of Glucosamine-6-phosphate Synthase from Escherichia coli

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10.1016/S0969-2126(96)00087-1

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