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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Chemical Compound Review: 

Ala-His     (2R)-2-[[(2S)-2- aminopropanoyl]amino]-3...

Synonyms: SureCN3916119, AC1O529S
 
 
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High impact information on Ala-His

  • Substitution of Phe393 by Ala, His, Tyr, and Trp has allowed us to modulate the reduction potential of the heme, while retaining the structural integrity of the enzyme's active site [1].
  • The His-epsilon Ahx-beta Ala-His tetrapeptide also inhibited purified human MMP-2 and MMP-9 and the corresponding enzymes present in conditioned media from human tumour cells [2].
  • The complex formation between Ala-His and H2VO4- in water has also been investigated (by 51V NMR); the formation constant at pH 7.2 amounts to 266(28) M-1 [3].
  • Mutation of Trp1035 to Leu, Ala, His or Tyr caused complete inactivation, whereas mutation of Glu1033 to Ala enhanced activity [4].
  • The reactions between some Ni(II) oligopeptides (Gly-His-Lys, (Gly)4, Asp-Ala-His-Lys, Gly-Gly-His, beta Ala-His, and serum albumin) and reduced oxygen species have been characterized by spin-trapping experiments using DMPO and Me2SO [5].
 

Gene context of Ala-His

  • From DNA-sequencing, 21 of 35 (60%) exhibited single-point mutations in different positions, at Ala90Val, Ser91Pro, and Asp94(Gly/Ala/His/Asn); and one novel mutation position at Gly88Cys in the gyrA gene and Asp495Asn in the gyrB gene [6].

References

  1. Oxygen activation and electron transfer in flavocytochrome P450 BM3. Ost, T.W., Clark, J., Mowat, C.G., Miles, C.S., Walkinshaw, M.D., Reid, G.A., Chapman, S.K., Daff, S. J. Am. Chem. Soc. (2003) [Pubmed]
  2. Selection of a histidine-containing inhibitor of gelatinases through deconvolution of combinatorial tetrapeptide libraries. Ferry, G., Boutin, J.A., Atassi, G., Fauchère, J.L., Tucker, G.C. Mol. Divers. (1997) [Pubmed]
  3. (Model) studies on vanadate-dependent bromo/iodoperoxidase from Ascophyllum nodosum. VO2+ is not incorporated into the active site. Knüttel, K., Müller, A., Rehder, D., Vilter, H., Wittneben, V. FEBS Lett. (1992) [Pubmed]
  4. Conserved amino acids at the C-terminus of rat phospholipase D1 are essential for enzymatic activity. Xie, Z., Ho, W.T., Exton, J.H. Eur. J. Biochem. (2000) [Pubmed]
  5. Redox chemistry of complexes of nickel(II) with some biologically important peptides in the presence of reduced oxygen species: an ESR study. Cotelle, N., Trémolières, E., Bernier, J.L., Catteau, J.P., Hénichart, J.P. J. Inorg. Biochem. (1992) [Pubmed]
  6. Mutations in the gyrA and gyrB genes of fluoroquinolone-resistant Mycobacterium tuberculosis from TB patients in Thailand. Pitaksajjakul, P., Wongwit, W., Punprasit, W., Eampokalap, B., Peacock, S., Ramasoota, P. Southeast Asian J. Trop. Med. Public Health (2005) [Pubmed]
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