6.3.4.15	A43G	catalytic efficiency is 2fold lower than catalytic efficiency of wild-type enzyme	-, 671759	
6.3.4.15	D571N	naturally occuring mutation, important in positioning K579 in the AMP binding site	691104	
6.3.4.15	D615Y	naturally occuring mutation in the loop between alpha3 and beta6 that cover AMP, may coordinate oxygens of the AMP phosphate	691104	
6.3.4.15	D634Y	naturally occuring mutation of a solvent exposed residue, distal to active site on alpha4 and alpha5, respectively	691104	
6.3.4.15	D715G	naturally occuring mutation on beta9, may be involved in capping and stabilising the catalytic domain structure	691104	
6.3.4.15	DELTA1-81	elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity	-, 745788	
6.3.4.15	DELTA1-81	elimination of N-terminal domain plus part of the central domain, loss of ligase activity	-, 746268	
6.3.4.15	DELTA2-63	elimination of N-terminal domain, mutant shows normal ligase activity	-, 746268	
6.3.4.15	DELTA2-65	elimination of N-terminal domain, complete loss of ligase activity	-, 745788	
6.3.4.15	DELTA2-65	elimination of N-terminal domain, mutant shows normal ligase activity	-, 746268	
6.3.4.15	DELTA2-74	elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity	-, 745788	
6.3.4.15	F123G	the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme	-, 728338	
6.3.4.15	F123R	the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme	-, 728338	
6.3.4.15	G115S	site-directed mutagenesis	653788	
6.3.4.15	G115S	site-directed mutagenesis, the mutant enzyme shows a highly increased rate of biotinyl-5'-AMP intermediate formation, but no release of the intermediate	666851	
6.3.4.15	G518E	naturally occuring mutation close to the active site and part of the ligand-binding loop, the mutation may not allow as much flexibility of this loop. As part of the hydrophobic pocket, making this polar residue would perturb biotin binding	691104	
6.3.4.15	G581S	naturally occuring mutation of a residue involved in hydrophobic interactions with biotin in the binding pocket	691104	
6.3.4.15	G582R	naturally occuring mutation of a residue involved in hydrophobic interactions with biotin in the binding pocket	691104	
6.3.4.15	I11V/P85S/ M157T/K163E/I224T	17fold increase in the ability to use desthiobiotin as a substrate	744546	
6.3.4.15	I272X	site-directed mutagenesis	653788	
6.3.4.15	K122E	site-directed mutagenesis	653788	
6.3.4.15	K138S	inactive	-, 746392	
6.3.4.15	K277E	site-directed mutagenesis	653788	
6.3.4.15	K283E	site-directed mutagenesis	653788	
6.3.4.15	K321E	site-directed mutagenesis	653788	
6.3.4.15	L237P	the mutant shows reduced catalytic activity compared to the wild-type enzyme	691104	
6.3.4.15	L470S	naturally occuring mutation in an unstructured loop distal to the ligand-binding site	691104	
6.3.4.15	M157T	2-3fold increase in kcat value for desthiobiotin as a substrate	744546	
6.3.4.15	additional information	construction of biotinylated magnetic nanoparticles, with or without introduced strepatavidin, by displaying biotin acceptor peptide or biotin carboxyl carrier protein, BCCP, on the surface of bacterial magnetic particles for analysis of in vitro biotinylation, method development and evaluation, overview	-, 690542	
6.3.4.15	additional information	disruption of BPL affects important metabolic pathways such as fatty acid biosynthesis and gluconeogenesis	-, 690627	
6.3.4.15	additional information	HCS mutants with deletions up to Ala235 or Thr266 still show catalytic activity and can complement an enzyme-deficient Escherichia coli birA- strain. Enzyme deficiency can cause symptoms like ketoacidosis, feeding difficulties, hypotonia, seizures, developmental delay and dermal abnormalities such as rashes, dryness of the skin and alopecia, multiple carboxylase deficiency is caused by a lack of activity of the biotin-dependent enzymes, phenotypes, overview. Molecular modelling of mutations causing HCS deficiency, detailed overview	691104	
6.3.4.15	additional information	mammalian cell surface proteins tagged with a 15-amino acid peptide, i.e. the AP-tag, are specifically biotinylated by Escherichia coli biotin ligase BirA, whereas endogenous proteins are not modified, overview. BirA labels the AP-tag specifically in different cellular compartments: at the cell surface, in the endoplasmic reticulum, in the cytosol, and in the nucleus of mammalian cells, including human, mouse, rat and hamster cell lines, and primary neuron culture. BirA labeling may also be used in living animals, for example in a transgenic mouse expressing cytosolic BirA, overview. Benefit of streptavidin labeling over Ab labeling, method development, detailed overview	694319	
6.3.4.15	additional information	mutational analysis, overview. The C-terminal 87 amino acids of biotin carboxyl carrier protein, i.e. BCCP-87, are recognised and biotinylated by BPL as well as full-length BCCP due to the fact that this peptide adopts the tertiary structure that is required for the interaction with BPL	691104	
6.3.4.15	Q41R/M157T/I224T/E215D/T225A	10fold increase in the ability to use desthiobiotin as a substrate	744546	
6.3.4.15	R118G	mutant shows enhanced self and promiscuous biotinylation	716697	
6.3.4.15	R118G	mutation of Arg118 to glycine in EcBPL causes altered affinity of BPL for biotin, increased dissociation rates for biotin and biotinyl-5'-AMP, and consequently, promiscuous biotinylation of inappropriate proteins	691104	
6.3.4.15	R118G	site-directed mutagenesis, the mutant enzyme shows a wider substrate specificity compared to the wild-type enzyme, the mutant biotinylates bovine serum albumin, chloramphenicol acetyltransferase, immunoglobin heavy and light chains, and RNase A in vitro, it also self-biotinylates in vivo and in vitro, the activity depends on proximity, distance to the substrate can be bridged by a linker like avidin, overview	666851	
6.3.4.15	R125A	the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme	-, 727901	
6.3.4.15	R125N	the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme	-, 727901	
6.3.4.15	R182E	site-directed mutagenesis	653788	
6.3.4.15	R212E	site-directed mutagenesis	653788	
6.3.4.15	R213E	site-directed mutagenesis	653788	
6.3.4.15	R317E	site-directed mutagenesis	653788	
6.3.4.15	R40G	site-directed mutagenesis, the structure of the mutant enzyme in both the ligand-free and biotin-bound forms reveals that the mutated loop has collapsed, thus hindering ATP binding. The mutant is catalytically active but shows poor substrate specificity. The affinity for biotin is reduced 3.5fold by the R40G mutation, but binding of ATP to mutant R40G is very weak in the absence or in the presence of biotin. Comparison to the equivalent mutant of Escherichia coli BirA, overview	705137	
6.3.4.15	R48A/K111A	site-directed mutagenesis, comparison of the nucleotide binding mode in the double mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant. Interface charge distribution in the double mutant complex, overview	-, 693053	
6.3.4.15	R48K	site-directed mutagenesis, comparison of the nucleotide binding mode in the mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant	-, 693053	
6.3.4.15	R508W/N511K	naturally occuring mutation of a residue critical in loop covering the ligand-binding site. R508 co-ordinates to the backbone carbonyl N712 to form a salt bridge, removing this would result in a more flexible loop, analogous to EcBPL R118 and R121 that co-ordinate oxygens within the AMP phosphate group	691104	
6.3.4.15	R69A	the binding constant for biotin is nearly the same as that observed for the wild type protein. Mutant does not undergo self-botinylation	716697	
6.3.4.15	T462I	naturally occuring mutation in an unstructured loop distal to the ligand-binding site	691104	
6.3.4.15	V547G	naturally occuring mutation of a buried hydrophobic residue in alpha2 that reside near the AMP-binding beta5 strand	691104	
6.3.4.15	V550M	naturally occuring mutation of a buried hydrophobic residue in alpha2 that reside near the AMP-binding beta5 strand	691104	
6.3.4.15	Y456C	naturally occuring mutation in an unstructured loop distal to the ligand-binding site	691104