Maltase

Alfa-glicosidase
Identificadores
Número EC	3.2.1.20
Número CAS	9001-42-7
Bases de datos
IntEnz	vista de IntEnz
BRENDA	entrada de BRENDA
ExPASy	vista de NiceZyme
KEGG	entrada de KEGG
MetaCyc	vía metabólica
PRIAM	perfil
Estruturas PDB	RCSB PDB PDBe PDBj PDBsum
Procura
PMC	artigos
PubMed	artigos
NCBI Protein	procura

A maltase (EC 3.2.1.20), tamén chamada alfa-glicosidase, glicoinvertase, glicosidosacarase, maltase-glicoamilase, alfa-glicopiranosidase, glicosidoinvertase, alfa-D-glicosidase, alfa-glicósido hidrolase, alfa-1,4-glicosidase, ou alfa-D-glicósido glicohidrolase, é un encima que hidroliza o disacárido maltosa, orixinando as dúas unidades de glicosa que a forman.^[1]^[2]^[3]^[4]^[5]^[6] Este encima encóntrase en plantas, bacterias, lévedos e animais. O encima hidroliza os enlaces O-glicosídicos alfa (1-4). No home encóntrase no epiitelio interno do intestino. Hai outros encimas alfa-glicosidases co mesmo número EC noutros tecidos.

Notas editar

↑ "Maltase - Definition from the Merriam-Webster Online Dictionary". Consultado o 2009-04-06.
↑ Bruni, C.B., Sica, V., Auricchio, F. and Covelli, I. (1970). "Further kinetic and structural characterization of the lysosomal α-D-glucoside glucohydrolase from cattle liver". Biochim. Biophys. Acta 212 (3): 470–477. PMID 5466143.
↑ Flanagan, P.R. and Forstner, G.G. (1978). "Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH". Biochem. J. 173 (2): 553–563. PMID 29602.
↑ Larner, J. (1960). "Other glucosidases". En Boyer, P.D., Lardy, H. and Myrbäck, K. The Enzymes 4 (2nd ed.). New York: Academic Press. pp. 369–378.
↑ Sivikami, S. and Radhakrishnan, A.N. (1973). "Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200". Indian J. Biochem. Biophys. 10 (4): 283–284. PMID 4792946.
↑ Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M. (1982). "Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity". Eur. J. Biochem. 126: 559–568. PMID 6814909. doi:10.1111/j.1432-1033.1982.tb06817.x.

Véxase tamén editar

Outros artigos editar

Ligazóns externas editar

Maltases Medical Subject Headings (MeSH) na Biblioteca Nacional de Medicina dos EUA.
Estrutura e evolución da maltase-glicoamilase e a sacarase-isomaltase de mamífero

[urlMaltase_-_Definition_from_the_Merriam-Webster_Online_Dictionary-1] "Maltase - Definition from the Merriam-Webster Online Dictionary". Consultado o 2009-04-06.

[2] Bruni, C.B., Sica, V., Auricchio, F. and Covelli, I. (1970). "Further kinetic and structural characterization of the lysosomal α-D-glucoside glucohydrolase from cattle liver". Biochim. Biophys. Acta 212 (3): 470–477. PMID 5466143.

[3] Flanagan, P.R. and Forstner, G.G. (1978). "Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH". Biochem. J. 173 (2): 553–563. PMID 29602.

[4] Larner, J. (1960). "Other glucosidases". En Boyer, P.D., Lardy, H. and Myrbäck, K. The Enzymes 4 (2nd ed.). New York: Academic Press. pp. 369–378.

[5] Sivikami, S. and Radhakrishnan, A.N. (1973). "Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200". Indian J. Biochem. Biophys. 10 (4): 283–284. PMID 4792946.

[6] Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M. (1982). "Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity". Eur. J. Biochem. 126: 559–568. PMID 6814909. doi:10.1111/j.1432-1033.1982.tb06817.x.

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