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・ N-Methylaniline
・ N-Methylcarfentanil
・ N-methylcoclaurine 3'-monooxygenase
・ N-Methylconiine
・ N-Methylephedrine
・ N-Methylethanolamine
・ N-Methylformamide
・ N-Acetylmannosamine
・ N-Acetylmescaline
・ N-Acetylmuramic acid
・ N-acetylmuramic acid 6-phosphate etherase
・ N-acetylmuramoyl-L-alanine amidase
・ N-acetylneuraminate 4-O-acetyltransferase
・ N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
・ N-acetylneuraminate epimerase
N-acetylneuraminate lyase
・ N-acetylneuraminate synthase
・ N-Acetylneuraminic acid
・ N-acetylneuraminylgalactosylglucosylceramide b-1,4-N-acetylgalactosaminyltransferase
・ N-acetylornithine carbamoyltransferase
・ N-acetylphosphatidylethanolamine-hydrolysing phospholipase D
・ N-Acetylprocainamide
・ N-Acetylserotonin
・ N-acetylserotonin O-methyltransferase-like protein
・ N-Acetyltalosaminuronic acid
・ N-acetyltransferase
・ N-acetyltransferase 1
・ N-acetyltransferase 2
・ N-Acyl homoserine lactone
・ N-acyl phosphatidylethanolamine-specific phospholipase D


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N-acetylneuraminate lyase : ウィキペディア英語版
N-acetylneuraminate lyase

In enzymology, a N-acetylneuraminate lyase () is an enzyme that catalyzes the chemical reaction
:N-acetylneuraminate \rightleftharpoons N-acetyl-D-mannosamine + pyruvate
Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate.
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming). Other names in common use include N-acetylneuraminic acid aldolase, acetylneuraminate lyase, sialic aldolase, sialic acid aldolase, sialate lyase, N-acetylneuraminic aldolase, neuraminic aldolase, N-acetylneuraminate aldolase, neuraminic acid aldolase, N-acetylneuraminic acid aldolase, neuraminate aldolase, N-acetylneuraminic lyase, N-acetylneuraminic acid lyase, NPL, NALase, NANA lyase, acetylneuraminate pyruvate-lyase, and N-acetylneuraminate pyruvate-lyase. This enzyme participates in aminosugars metabolism.
==Structural studies==

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .

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