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Biochem Biophys Res Commun. 1991 Nov 27;181(1):87-94.

Sequence conservation of the catalytic regions of amylolytic enzymes in maize branching enzyme-I.

Author information

1
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.

Abstract

We have identified cDNA clones encoding branching enzyme-I (BE-I) from a maize kernel cDNA library. The combined nucleotide sequence of the cDNAs indicates that maize BE-I is initially synthesized as a precursor protein with a putative 64-residue transit peptide at the amino terminus, and that the mature enzyme contains 759 amino acid residues with a calculated molecular mass of 86,236 Da. The four regions, which constitute the catalytic site of amylolytic enzymes, are conserved in the sequences of BE-I and bacterial branching enzymes. This result demonstrates that branching enzyme belongs to a family of the amylolytic enzymes. The BE-I gene is highly expressed in the early stages of kernel development, and the level of the message concentration decreases slowly as kernel maturation proceeds.

PMID:
1720313
DOI:
10.1016/s0006-291x(05)81385-3
[Indexed for MEDLINE]

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