scholarly journals A Missing Enzyme in Thiamin Thiazole Biosynthesis: Identification of TenI as a Thiazole Tautomerase

2011 ◽  
Vol 133 (24) ◽  
pp. 9311-9319 ◽  
Author(s):  
Amrita B. Hazra ◽  
Ying Han ◽  
Abhishek Chatterjee ◽  
Yang Zhang ◽  
Rung-Yi Lai ◽  
...  
Keyword(s):  
Missing Enzyme

HISTIDINEMIA DISCOVERED BY URINE SCREENING AFTER RENAL TRANSPLANTATION

PEDIATRICS ◽  
1970 ◽  
Vol 46 (1) ◽  
pp. 47-53
Author(s):  
David Rosenblatt ◽  
Fazl Mohyuddin ◽  
Charles R. Scriver
Keyword(s):  
Renal Transplantation ◽  
Inborn Errors Of Metabolism ◽  
Autosomal Recessive ◽  
Old French ◽  
Host Cells ◽  
French Canadian ◽  
Inborn Errors ◽  
Urine Screening ◽  
Missing Enzyme ◽  
Cadaver Kidney

Histidinemia has been discovered by urine screening in a 17-year-old French-Canadian female, who has a single, transplanted cadaver kidney. She has normal intelligence and speech. Activity of L-histidine, ammonia-lyase (histidase) was absent in stratum corneum and other organs. The transplanted kidney handled histidine and its metabolites efficiently. The trait was inherited as an autosomal recessive, with both parents exhibiting deficient histidase activity. The patient is ently chimerical for histidase activity. The host cells contain no activity; the implanted kidney presumably contains the normal but ineffective amount of histidase activity. Homozygotes with certain inborn errors of metabolism might benefit in the future from "transplant chimerism" if the appropriate organ containing the missing enzyme were implanted.

scholarly journals Altered molecular size of N-acetylglucosamine 1-phosphotransferase in I-cell disease and pseudo-Hurler polydystrophy

1987 ◽  
Vol 248 (3) ◽  
pp. 697-701 ◽  
Author(s):  
Y Ben-Yoseph ◽  
M Potier ◽  
D A Mitchell ◽  
B A Pack ◽  
S B Melançon ◽  
...  
Keyword(s):  
Cell Lines ◽  
Molecular Size ◽  
Normal Activity ◽  
Complementation Group ◽  
Enzyme Molecule ◽  
Cell Disease ◽  
Acceptor Substrate ◽  
Golgi Membranes ◽  
Missing Enzyme ◽  
Normal Enzyme

The size of the mutant N-acetylglucosamine 1-phosphotransferase in Golgi membranes from fibroblasts of patients with I-cell disease and classical pseudo-Hurler polydystrophy, which comprised one complementation group characterized by deficiency towards both artificial and natural acceptor substrates, was significantly smaller than the normal enzyme, 151-174 kDa compared with 225-278 kDa. The size of the mutant enzyme from cell lines of patients with variant forms of pseudo-Hurler polydystrophy, which comprised another complementation group characterized by normal activity towards mono- and oligo-saccharide substrates, was significantly larger than the normal enzyme, ranging from 321 to 356 kDa in two families and from 528 to 547 kDa in a third family. These findings suggest that the mutations in I-cell disease and classical pseudo-Hurler polydystrophy result in a missing enzyme component, which renders the enzyme catalytically inefficient toward any type of acceptor substrate. In contrast, the mutations in the variant forms of pseudo-Hurler polydystrophy produce a larger enzyme molecule which is active toward small substrates but is incapable of binding natural lysosomal glycoprotein substrates.

Missing Enzyme May Cause Alzheimer’s Tangles in Brain

2003 ◽  
Vol 38 (17) ◽  
pp. 23-23
Author(s):  
Joan Arehart-Treichel
Keyword(s):  
Missing Enzyme

scholarly journals Prediction of missing enzyme genes in a bacterial metabolic network

FEBS Journal ◽  
2007 ◽  
Vol 274 (9) ◽  
pp. 2262-2273 ◽  
Author(s):  
Yoshihiro Yamanishi ◽  
Hisaaki Mihara ◽  
Motoharu Osaki ◽  
Hisashi Muramatsu ◽  
Nobuyoshi Esaki ◽  
...  
Keyword(s):  
Metabolic Network ◽  
Missing Enzyme

Brain fix: Stem cells supply missing enzyme

Science News ◽  
2007 ◽  
Vol 171 (11) ◽  
pp. 163-163
Author(s):  
Brian Vastag
Keyword(s):  
Stem Cells ◽  
Missing Enzyme
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