The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri.
A novel post-translational protein modification has recently been described in two human sulfatases, by which a cysteine is replaced by a serinesemialdehyde (2-amino-3-oxopropionic acid) residue [Schmidt, B., Selmer, T., Ingendoh, A. & von Figura, K. (1995) Cell 82, 271-278]. This cysteine is conserved among all known eukaryotic sulfatases. Here we report the presence of this modification in arylsulfatase from the green alga Volvox carteri. The evolutionary conservation of this novel protein modification between sulfatases of V. carteri and man lends further support to the assumption that this modification is required for the catalytic activity of sulfatases and may be present in all sulfatases of eukaryotic origin.
Selmer
T
T
Universität Göttingen, Germany.
Hallmann
A
A
Schmidt
B
B
Sumper
M
M
von Figura
K
K
D000409:Alanine / Q000031:analogs & derivatives / Q000032:analysis; D000447:Aldehydes / Q000032:analysis; D000595:Amino Acid Sequence; D001192:Arylsulfatases / Q000737:chemistry* / Q000302:isolation & purification; D001894:Borohydrides; D000460:Chlorophyta / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D017124:Conserved Sequence; D003545:Cysteine / Q000032:analysis*; D019143:Evolution, Molecular; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D014357:Trypsin / Q000378:metabolism
C094933:2-amino-3-oxopropionic acid; D000447:Aldehydes; D001894:Borohydrides; D010446:Peptide Fragments; C025364:sodium borohydride; D001192:Arylsulfatases; D014357:Trypsin; D003545:Cysteine; D000409:Alanine