assay
98%
optical activity
[α]23/D −38.4°, c = 3 in H2O
mp
282 °C (dec.) (lit.)
SMILES string
N[C@@H](Cc1c[nH]cn1)C(O)=O
InChI
1S/C6H9N3O2/c7-5(6(10)11)1-4-2-8-3-9-4/h2-3,5H,1,7H2,(H,8,9)(H,10,11)/t5-/m0/s1
InChI key
HNDVDQJCIGZPNO-YFKPBYRVSA-N
Biochem/physiol Actions
组胺的前体,经组氨酸脱羧酶作用可生成组胺。
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Claudia Temperini et al.
Bioorganic & medicinal chemistry letters, 16(19), 5152-5156 (2006-07-28)
The X-ray crystallographic structure for the adduct of an activator with human carbonic anhydrase isozyme I (hCA I) is reported. L-Histidine binds deep within the enzyme active site, participating in a network of hydrogen bonds involving its carboxylate moiety and
Marie-Rose Abdo et al.
Bioorganic & medicinal chemistry letters, 19(9), 2440-2443 (2009-04-07)
Activation of the human carbonic anhydrase (CA, EC 4.2.1.1) isozymes I, II (cytosolic) and IX (transmembrane, tumor-associated isoform) with a series of arylsulfonylhydrazido-l-histidines incorporating 4-substituted-phenyl, pentafluorophenyl- and beta-naphthyl moieties was investigated. The compounds showed a weak hCA I activation profile
Claudia Temperini et al.
Bioorganic & medicinal chemistry letters, 15(23), 5136-5141 (2005-10-11)
Activation of the carbonic anhydrase (CA, EC 4.2.1.1) isoforms hCA I, II, and IV with l-histidine and some of its derivatives has been investigated by kinetic and X-ray crystallographic methods. l-His was a potent activator of isozymes I and IV