Amino acid homologies between human biotinidase and bacterial aliphatic amidases: Putative identification of the active site of biotinidase

K. L. Swango; J. Hymes; P. Brown; B. Wolf

doi:10.1006/mgme.2000.2959

Amino acid homologies between human biotinidase and bacterial aliphatic amidases: Putative identification of the active site of biotinidase

K. L. Swango, J. Hymes, P. Brown, B. Wolf^*

^*Corresponding author for this work

Pediatrics

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

A search of protein databases revealed amino acid homologies among human biotinidase, bacterial aliphatic amidases, and bacterial and plant nitrilases. Amino acids YRK_210-212 of biotinidase are conserved among the enzyme families. This homology and naturally occurring mutations that cause biotinidase deficiency suggest that this region is essential for enzyme activity land is conserved from bacteria. Cys₂₄₅ is likely the cysteine in the active site of biotinidase. (C) 2000 Academic Press.

Original language	English (US)
Pages (from-to)	111-115
Number of pages	5
Journal	Molecular Genetics and Metabolism
Volume	69
Issue number	2
DOIs	https://doi.org/10.1006/mgme.2000.2959
State	Published - Feb 2000

Funding

This work was supported in part by Grant 33840 from the National Institutes of Health.

Keywords

Active site
Aliphatic amidase
Biotinidase
Nitrilase

ASJC Scopus subject areas

Genetics
Endocrinology
Molecular Biology
Biochemistry
Endocrinology, Diabetes and Metabolism

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1006/mgme.2000.2959

Cite this

@article{1d33afe46d6a468d9b2b1f954ac75840,

title = "Amino acid homologies between human biotinidase and bacterial aliphatic amidases: Putative identification of the active site of biotinidase",

abstract = "A search of protein databases revealed amino acid homologies among human biotinidase, bacterial aliphatic amidases, and bacterial and plant nitrilases. Amino acids YRK210-212 of biotinidase are conserved among the enzyme families. This homology and naturally occurring mutations that cause biotinidase deficiency suggest that this region is essential for enzyme activity land is conserved from bacteria. Cys245 is likely the cysteine in the active site of biotinidase. (C) 2000 Academic Press.",

keywords = "Active site, Aliphatic amidase, Biotinidase, Nitrilase",

author = "Swango, {K. L.} and J. Hymes and P. Brown and B. Wolf",

note = "Funding Information: This work was supported in part by Grant 33840 from the National Institutes of Health.",

year = "2000",

month = feb,

doi = "10.1006/mgme.2000.2959",

language = "English (US)",

volume = "69",

pages = "111--115",

journal = "Molecular Genetics and Metabolism",

issn = "1096-7192",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Amino acid homologies between human biotinidase and bacterial aliphatic amidases

T2 - Putative identification of the active site of biotinidase

AU - Swango, K. L.

AU - Hymes, J.

AU - Brown, P.

AU - Wolf, B.

N1 - Funding Information: This work was supported in part by Grant 33840 from the National Institutes of Health.

PY - 2000/2

Y1 - 2000/2

N2 - A search of protein databases revealed amino acid homologies among human biotinidase, bacterial aliphatic amidases, and bacterial and plant nitrilases. Amino acids YRK210-212 of biotinidase are conserved among the enzyme families. This homology and naturally occurring mutations that cause biotinidase deficiency suggest that this region is essential for enzyme activity land is conserved from bacteria. Cys245 is likely the cysteine in the active site of biotinidase. (C) 2000 Academic Press.

AB - A search of protein databases revealed amino acid homologies among human biotinidase, bacterial aliphatic amidases, and bacterial and plant nitrilases. Amino acids YRK210-212 of biotinidase are conserved among the enzyme families. This homology and naturally occurring mutations that cause biotinidase deficiency suggest that this region is essential for enzyme activity land is conserved from bacteria. Cys245 is likely the cysteine in the active site of biotinidase. (C) 2000 Academic Press.

KW - Active site

KW - Aliphatic amidase

KW - Biotinidase

KW - Nitrilase

UR - http://www.scopus.com/inward/record.url?scp=0034086054&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034086054&partnerID=8YFLogxK

U2 - 10.1006/mgme.2000.2959

DO - 10.1006/mgme.2000.2959

M3 - Article

C2 - 10720437

AN - SCOPUS:0034086054

SN - 1096-7192

VL - 69

SP - 111

EP - 115

JO - Molecular Genetics and Metabolism

JF - Molecular Genetics and Metabolism

IS - 2

ER -

Amino acid homologies between human biotinidase and bacterial aliphatic amidases: Putative identification of the active site of biotinidase

Abstract

Funding

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this