Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase. - Test2 - elhamkhani - TriplyDB

Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase.

Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase.

http://www.wikidata.org/entity/Q35221662

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Artemisinin-based antimalarial research: application of biotechnology to the production of artemisinin, its mode of action, and the mechanism of resistance of Plasmodium parasites An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism.

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Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase.

http://www.wikidata.org/entity/Q35221662

description

2015 nî lūn-bûn

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2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի փետրվարին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

@zh-hk

2015年論文

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2015年論文

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2015年论文

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name

Kinetic mechanism and the rate ...... rine hydroxymethyltransferase.

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Kinetic mechanism and the rate ...... rine hydroxymethyltransferase.

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type

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Kinetic mechanism and the rate ...... rine hydroxymethyltransferase.

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Kinetic mechanism and the rate ...... rine hydroxymethyltransferase.

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Kinetic mechanism and the rate ...... rine hydroxymethyltransferase.

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Kinetic mechanism and the rate ...... rine hydroxymethyltransferase.

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JBC.M114.612275

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Journal of Biological Chemistry

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Kinetic mechanism and the rate ...... rine hydroxymethyltransferase.

@en

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Jeerus Sucharitakul

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Pasupat Krasatong

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Penchit Chitnumsub

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Somchart Maenpuen

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Ubolsree Leartsakulpanich

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Watcharee Amornwatcharapong

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P2860

Distinct biochemical properties of human serine hydroxymethyltransferase compared with the Plasmodium enzyme: implications for selective inhibition

Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate

Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase

Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism

Structure determination and biochemical studies on Bacillus stearothermophilus E53Q serine hydroxymethyltransferase and its complexes provide insights on function and enzyme memory

Importance of tyrosine residues of Bacillus stearothermophilus serine hydroxymethyltransferase in cofactor binding and L-allo-Thr cleavage

Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyltransferase: the role of Asn(341), Tyr(60) and Phe(351) in tetrahydrofolate binding

Characterization of Plasmodium falciparum serine hydroxymethyltransferase-A potential antimalarial target

The structure of Plasmodium falciparum serine hydroxymethyltransferase reveals a novel redox switch that regulates its activities.

Serine hydroxymethyltransferase: a model enzyme for mechanistic, structural, and evolutionary studies.

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13

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Pimchai Chaiyen

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25678710

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Plasmodium vivax

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