(Q43024362)

English

Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1.

scientific article published in December 1996

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scholarly article

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Europe PubMed Central

PubMed publication ID

12 November 2017

Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1. (English)

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

author name string

H S Ro

1

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

S P Hong

2

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Europe PubMed Central

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12 November 2017

H J Seo

3

1 reference

Europe PubMed Central

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12 November 2017

T Yoshimura

4

1 reference

Europe PubMed Central

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12 November 2017

N Esaki

5

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

K Soda

6

1 reference

Europe PubMed Central

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12 November 2017

H S Kim

7

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Europe PubMed Central

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12 November 2017

M H Sung

8

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Europe PubMed Central

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12 November 2017

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publication date

1 December 1996

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12 November 2017

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Europe PubMed Central

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12 November 2017

398

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12 November 2017

2-3

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Europe PubMed Central

PubMed publication ID

12 November 2017

141-145

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Europe PubMed Central

PubMed publication ID

12 November 2017

Staphylococcus haemolyticus contains two D-glutamic acid biosynthetic activities, a glutamate racemase and a D-amino acid transaminase

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Site-directed mutagenesis of the cysteinyl residues and the active-site serine residue of bacterial D-amino acid transaminase

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Rat liver aromatic L-amino acid decarboxylase: spectroscopic and kinetic analysis of the coenzyme and reaction intermediates

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: involvement of Tyr70 in stabilization of the catalytic intermediates.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

The mode of binding of pyridoxal 5′-phosphate in glycogen phosphorylase

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2896%2901222-7

21 January 2018

Identifiers

10.1016/S0014-5793(96)01222-7

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

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