3.5.1.122: protein N-terminal glutamine amidohydrolase
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For detailed information about protein N-terminal glutamine amidohydrolase, go to the full flat file.
Reaction
Synonyms
C8orf32, Cg8253, CT1, FLJ10204, Gln-specific amino-terminal (Nt)-amidase, glutamine-specific N-terminal amidase, hNtaq1, human N-terminal glutamine amidohydrolase isoform 1, N-terminal amidase, Nt-amidase, NTA1, Ntaq, NTAQ1, NtQ-amidase, Wdyhv1, yNta1
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Subunits
Subunits on EC 3.5.1.122 - protein N-terminal glutamine amidohydrolase
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monomer
in solution, yNta1 is a monomer containing 14 beta-strands, 11 alpha-helices, and three 310-helices. The core region of the enzyme shows antiparallel and parallel mixed beta-sheets surrounded by helices, and these sixstranded beta-sheets face each other
additional information
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x * 40000, CT1 polypeptide fragment of glucosamine-6-phosphate synthase, SDS-PAGE
the enzyme structure reveals a monomeric globular protein with alpha-beta-alpha three-layer sandwich architecture. The catalytic triad located in the active site, Cys-His-Asp, is highly conserved among Ntaq family and transglutaminases from diverse organisms. Substrate binding mode of hNtaq1 with the N-terminus of a symmetry-related Ntaq1 molecule bound in the substrate binding cleft
additional information
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the enzyme structure reveals a monomeric globular protein with alpha-beta-alpha three-layer sandwich architecture. The catalytic triad located in the active site, Cys-His-Asp, is highly conserved among Ntaq family and transglutaminases from diverse organisms. Substrate binding mode of hNtaq1 with the N-terminus of a symmetry-related Ntaq1 molecule bound in the substrate binding cleft