Sequence of 1A1C_MALDO

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
1-aminocyclopropane-1-carboxylate synthase
P37821
Malus domestica
473
53251
Reaction
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine
Sequences with same EC No.
Sequence
show sequence in fasta format
  0 MRMLSRNATF NSHGQDSSYF LGWQEYEKNP YHEVHNTNGI IQMGLAENQL CFDLLESWLA
 60 KNPEAAAFKK NGESIFAELA LFQDYHGLPA FKKAMVDFMA EIRGNKVTFD PNHLVLTAGA
120 TSANETFIFC LADPGEAVLI PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITETALEE
180 AYQEAEKRNL RVKGVLVTNP SNPLGTTMTR NELYLLLSFV EDKGIHLISD EIYSGTAFSS
240 PSFISVMEVL KDRNCDENSE VWQRVHVVYS LSKDLGLPGF RVGAIYSNDD MVVAAATKMS
300 SFGLVSSQTQ HLLSAMLSDK KLTKNYIAEN HKRLKQRQKK LVSGLQKSGI SCLNGNAGLF
360 CWVDMRHLLR SNTFEAEMEL WKKIVYEVHL NISPGSSCHC TEPGWFRVCF ANLPERTLDL
420 AMQRLKAFVG EYYNVPEVNG GSQSSHLSHS RRQSLTKWVS RLSFDDRGPI PGR
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
183
Lay-Yee M.,Knighton M.L.
A full-length cDNA encoding 1-aminocyclopropane-1-carboxylate synthase from apple.
Plant Physiol.
107
1017-1018
1995
185
Dong J.G.,Kim W.T.,Yip W.K.,Thompson G.A.,Li L.,Bennett A.B.,Yang S.F.
Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate synthase and expression of its mRNA in ripening apple fruit.
Planta
185
38-45
1991
186
White M.F.,Vasquez J.,Yang S.F.,Kirsch J.F.
Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.
Proc. Natl. Acad. Sci. U.S.A.
91
12428-12432
1994
187
Li Y.,Feng L.,Kirsch J.F.
Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase.
Biochemistry
36
15477-15488
1997
188
Feng L.,Kirsch J.F.
L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase.
Biochemistry
39
2436-2444
2000
189
McCarthy D.L.,Capitani G.,Feng L.,Gruetter M.G.,Kirsch J.F.
Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant.
Biochemistry
40
12276-12284
2001
190
Ko S.,Eliot A.C.,Kirsch J.F.
S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase.
Arch. Biochem. Biophys.
421
85-90
2004
191
Capitani G.,Hohenester E.,Feng L.,Storici P.,Kirsch J.F.,Jansonius J.N.
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene.
J. Mol. Biol.
294
745-756
1999
192
Capitani G.,McCarthy D.L.,Gut H.,Grutter M.G.,Kirsch J.F.
Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate.
J. Biol. Chem.
277
49735-49742
2002
193
Capitani G.,Eliot A.C.,Gut H.,Khomutov R.M.,Kirsch J.F.,Gruetter M.G.
Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
Biochim. Biophys. Acta
1647
55-60
2003
194
Capitani G.,Tschopp M.,Eliot A.C.,Kirsch J.F.,Gruetter M.G.
Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine.
FEBS Lett.
579
2458-2462
2005
195
Schaerer M.A.,Eliot A.C.,Gruetter M.G.,Capitani G.
Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy.
FEBS Lett.
585
111-114
2011