Selective loss of either the epimerase or kinase activity of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase due to site-directed mutagenesis based on sequence alignments (Q42058001)

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scientific article published on October 1999

Language	Label	Description	Also known as
English	Selective loss of either the epimerase or kinase activity of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase due to site-directed mutagenesis based on sequence alignments	scientific article published on October 1999

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

Selective loss of either the epimerase or kinase activity of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase due to site-directed mutagenesis based on sequence alignments (English)

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

sequence alignment

1 reference

based on heuristic

inferred from title

author name string

Effertz K

1

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

Hinderlich S

2

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Europe PubMed Central

PubMed publication ID

15 October 2017

Reutter W

3

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Europe PubMed Central

PubMed publication ID

15 October 2017

language of work or name

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publication date

1 October 1999

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Europe PubMed Central

PubMed publication ID

15 October 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

15 October 2017

274

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Europe PubMed Central

PubMed publication ID

15 October 2017

40

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

28771-28778

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

Cell adhesion molecules: implications for a molecular histology

1 reference

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Synthesis, characterization and properties of sialylated catalase

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Asn-linked oligosaccharides in lectin-resistant tumor-cell mutants with varying metastatic potential.

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UDP-GlcNAc 2-epimerase: a regulator of cell surface sialylation

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THE FEEDBACK CONTROL OF SUGAR NUCLEOTIDE BIOSYNTHESIS IN LIVER

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21 January 2018

A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase

1 reference

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Tissue expression and amino acid sequence of murine UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase

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Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme

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Multiple sequence alignment with hierarchical clustering

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Active site residues of human brain hexokinase as studied by site-specific mutagenesis

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Purification and characterization of N-acetylglucosamine kinase from rat liver--comparison with UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase.

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Understanding enzyme superfamilies. Chemistry As the fundamental determinant in the evolution of new catalytic activities

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Dissociation of enzyme oligomers: a mechanism for allosteric regulation

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Primary structure and expression analysis of human UDP-N-acetyl-glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis

1 reference

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21 January 2018

Residues Putatively Involved in Binding of ATP and Glucose 6-Phosphate to a Mammalian Hexokinase: Site-Directed Mutation at Analogous Positions in the N- and C-Terminal Halves of the Type I Isozyme

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21 January 2018

Identifiers

10.1074/JBC.274.40.28771

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

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