Structural highlights
Function
MAP1_YEAST Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val.[HAMAP-Rule:MF_03174][1] [2] [3] [4] [5]
References
- ↑ Chen S, Vetro JA, Chang YH. The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae. Arch Biochem Biophys. 2002 Feb 1;398(1):87-93. PMID:11811952 doi:10.1006/abbi.2001.2675
- ↑ Vetro JA, Chang YH. Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo. J Cell Biochem. 2002;85(4):678-88. PMID:11968008 doi:10.1002/jcb.10161
- ↑ Dummitt B, Micka WS, Chang YH. N-terminal methionine removal and methionine metabolism in Saccharomyces cerevisiae. J Cell Biochem. 2003 Aug 1;89(5):964-74. PMID:12874831 doi:10.1002/jcb.10566
- ↑ Pasquini M, Grosjean N, Hixson KK, Nicora CD, Yee EF, Lipton M, Blaby IK, Haley JD, Blaby-Haas CE. Zng1 is a GTP-dependent zinc transferase needed for activation of methionine aminopeptidase. Cell Rep. 2022 May 17;39(7):110834. PMID:35584675 doi:10.1016/j.celrep.2022.110834
- ↑ Zuo S, Guo Q, Ling C, Chang YH. Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth. Mol Gen Genet. 1995 Jan 20;246(2):247-53. PMID:7862096 doi:10.1007/BF00294688
